{{위키데이터 속성 추적}}
{{다른 뜻}}
{{chembox
| name = 류신
| ImageFile1 = L-Leucine.svg
| ImageCaption1 = L-류신의 [[골격 구조식]]
| ImageFileL2 = File:Leucine-from-xtal-3D-bs-17.png
| ImageCaptionL2 = [[공-막대 모형]]<ref name="Binns">{{저널 인용| vauthors = Binns J, Parsons S, McIntyre GJ | title = Accurate hydrogen parameters for the amino acid L-leucine | journal = Acta Crystallographica Section B | volume = 72 | issue = Pt 6 | pages = 885–892 | date = December 2016 | pmid = 27910839 | doi = 10.1107/S2052520616015699 | hdl-access = free | hdl = 20.500.11820/c784fdaf-aa3a-48e4-86a2-d0a0bd7fdb7a | url = https://www.pure.ed.ac.uk/ws/files/36568495/20170523_Parsons_Leucine_0410.pdf }}</ref>
| ImageFileR2 = Leucine-from-xtal-3D-sf.png
| ImageCaptionR2 = [[공간채움 모형]]<ref name="Binns" />
| IUPACName = leucine
| OtherNames = 2-amino-4-methylpentanoic acid
|Section1={{Chembox Identifiers
| IUPHAR_ligand = 3312
| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}
| ChemSpiderID = 5880
| UNII_Ref = {{fdacite|correct|FDA}}
| UNII = GMW67QNF9C
| ChEMBL_Ref = {{ebicite|correct|EBI}}
| ChEMBL = 291962
| InChI = 1/C6H13NO2/c1-4(2)3-5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t5-/m0/s1
| InChIKey = ROHFNLRQFUQHCH-YFKPBYRVBU
| StdInChI_Ref = {{stdinchicite|correct|chemspider}}
| StdInChI = 1S/C6H13NO2/c1-4(2)3-5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t5-/m0/s1
| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}}
| StdInChIKey = ROHFNLRQFUQHCH-YFKPBYRVSA-N
| CASNo = 61-90-5
| CASNo_Ref = {{cascite|correct|CAS}}
| PubChem = 6106
| KEGG_Ref = {{keggcite|correct|kegg}}
| KEGG = D00030
| DrugBank_Ref = {{drugbankcite|correct|drugbank}}
| DrugBank = DB00149
| ChEBI_Ref = {{ebicite|correct|EBI}}
| ChEBI = 15603
| SMILES = CC(C)C[C@@H](C(=O)O)N
| SMILES1 = CC(C)C[C@@H](C(=O)[O-])[NH3+]
| SMILES1_Comment = 양쪽성 이온
}}
|Section2={{Chembox Properties
| C=6 | H=13 | N=1 | O=2
| Appearance = 
| Density = 
| MeltingPt = 
| BoilingPt =
| pKa=2.36 (카복실기), 9.60 (아미노기)<ref>Dawson, R.M.C., et al., ''Data for Biochemical Research'', Oxford, Clarendon Press, 1959.</ref>
| Solubility = 
| MagSus = -84.9·10<sup>−6</sup> cm<sup>3</sup>/mol}}
|Section3={{Chembox Hazards
| MainHazards = 
| FlashPt = 
| AutoignitionPt = }}
}}

'''류신'''({{llang|en|leucine}}, {{llang|de|leucin|로이신}}, {{문화어|로이신}}, 기호: '''Leu''' or '''L''')<ref>{{웹 인용| url = http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | title = Nomenclature and Symbolism for Amino Acids and Peptides | publisher = IUPAC-IUB Joint Commission on Biochemical Nomenclature | year = 1983 | access-date = 5 March 2018 | archive-url = https://web.archive.org/web/20081009023202/http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | archive-date = 9 October 2008 | url-status = dead }}</ref>은 [[단백질 생합성|단백질의 생합성]]에 사용되는 [[필수 아미노산]]이다. 류신은 α-[[아미노산]]이며, α-[[아미노기]](생물학적 조건에서 [[양성자화]]된 −NH<sub>3</sub><sup>+</sup> 형태), α-[[카복실기]](생물학적 조건에서 [[탈양성자화]]된 −COO<sup>−</sup> 형태) 및 곁사슬인 [[뷰틸기|아이소뷰틸기]]를 포함하고 있다. 류신은 [[비극성]] [[지방족 화합물|지방족]] 아미노산이다. 류신은 사람에게 [[필수 아미노산|필수적인 아미노산]]으로 신체에서 합성되지 않으며 음식을 통해 섭취해야 한다. 사람은 [[육류]], [[유제품]], 콩 제품, 기타 콩류와 같은 [[단백질]]을 함유한 식품으로부터 류신을 얻을 수 있다. 류신은 UUA, UUG, CUU, CUC, CUA, CUG [[코돈]]에 의해 [[유전 부호|암호화]]되어 있다.

[[발린]]과 [[아이소류신]]과 마찬가지로 류신은 [[가지사슬 아미노산]]이다. 류신 대사의 주요한 대사 최종 산물은 [[아세틸-CoA]]와 [[아세토아세트산]]이다. 따라서 류신은 [[리신]]과 함께 [[케톤체생성성 아미노산]]이다.<ref>{{서적 인용|url=https://books.google.com/books?id=sSyMAwAAQBAJ&pg=PA266|title=Biochemistry| vauthors = Ferrier DR |date=2013-05-24|publisher=Lippincott Williams & Wilkins|isbn=9781451175622|language=en}}</ref> 류신은 사람에서 가장 중요한 케톤체생성성 아미노산이다.<ref>{{서적 인용|url=https://books.google.com/books?id=X3DK4nWybaMC|title=Metabolic & Therapeutic Aspects of Amino Acids in Clinical Nutrition | edition = Second | vauthors = Cynober LA |date=2003-11-13|publisher=CRC Press|isbn=9780203010266|language=en|page=101}}</ref>

류신 및 류신의 소량 [[대사산물]]인 [[β-하이드록시 β-메틸뷰티르산]]은 사람에서 [[생물학적 활성|약리학적 활성]]을 나타내며, mTOR의 [[인산화]]를 통해 [[단백질 생합성|단백질의 생합성]]을 촉진하는 것으로 입증되었다.<ref name="Pimentel 2017 systematic review on HMB">{{저널 인용| vauthors = Silva VR, Belozo FL, Micheletti TO, Conrado M, Stout JR, Pimentel GD, Gonzalez AM | title = β-hydroxy-β-methylbutyrate free acid supplementation may improve recovery and muscle adaptations after resistance training: a systematic review | journal = Nutrition Research | volume = 45 | pages = 1–9 | date = September 2017 | pmid = 29037326 | doi = 10.1016/j.nutres.2017.07.008 | hdl-access = free | quote = HMB's mechanisms of action are generally considered to relate to its effect on both muscle protein synthesis and muscle protein breakdown (Figure 1) [2, 3]. HMB appears to stimulate muscle protein synthesis through an up-regulation of the mammalian/mechanistic target of rapamycin complex 1 (mTORC1), a signaling cascade involved in coordination of translation initiation of muscle protein synthesis [2, 4]. Additionally, HMB may have antagonistic effects on the ubiquitin–proteasome pathway, a system that degrades intracellular proteins [5, 6]. Evidence also suggests that HMB promotes myogenic proliferation, differentiation, and cell fusion [7].&nbsp;... Exogenous HMB-FA administration has shown to increase intramuscular anabolic signaling, stimulate muscle protein synthesis, and attenuate muscle protein breakdown in humans [2]. <!--Therefore, the anabolic and anti-catabolic properties of HMB-FA offer an appealing nutritional supplement for athletes participating in high-intensity, muscle damaging exercise.--> | hdl = 11449/170023 }}</ref><ref name="Pharmacology of HMB-FA in humans in vivo">{{저널 인용| vauthors = Wilkinson DJ, Hossain T, Hill DS, Phillips BE, Crossland H, Williams J, Loughna P, Churchward-Venne TA, Breen L, Phillips SM, Etheridge T, Rathmacher JA, Smith K, Szewczyk NJ, Atherton PJ | display-authors = 6 | title = Effects of leucine and its metabolite β-hydroxy-β-methylbutyrate on human skeletal muscle protein metabolism | journal = The Journal of Physiology | volume = 591 | issue = 11 | pages = 2911–23 | date = June 2013 | pmid = 23551944 | pmc = 3690694 | doi = 10.1113/jphysiol.2013.253203 | quote = The stimulation of MPS through mTORc1-signalling following HMB exposure is in agreement with pre-clinical studies (Eley et al. 2008).&nbsp;... Furthermore, there was clear divergence in the amplitude of phosphorylation for 4EBP1 (at Thr37/46 and Ser65/Thr70) and p70S6K (Thr389) in response to both Leu and HMB, with the latter showing more pronounced and sustained phosphorylation.&nbsp;...  Nonetheless, as the overall MPS response was similar, this cellular signalling distinction did not translate into statistically distinguishable anabolic effects in our primary outcome measure of MPS.&nbsp;... Interestingly, although orally supplied HMB produced no increase in plasma insulin, it caused a depression in MPB (−57%). Normally, postprandial decreases in MPB (of ~50%) are attributed to the nitrogen-sparing effects of insulin since clamping insulin at post-absorptive concentrations (5&nbsp;μU&nbsp;ml<sup>−1</sup>) while continuously infusing AAs (18&nbsp;g&nbsp;h<sup>−1</sup>) did not suppress MPB (Greenhaff et al. 2008), which is why we chose not to measure MPB in the Leu group, due to an anticipated hyperinsulinaemia (Fig. 3C). Thus, HMB reduces MPB in a fashion similar to, but independent of, insulin. These findings are in-line with reports of the anti-catabolic effects of HMB suppressing MPB in pre-clinical models, via attenuating proteasomal-mediated proteolysis in response to LPS (Eley et al. 2008). }}</ref>

== 식이 류신 ==
[[식품 첨가물]]로 사용되는 L-류신은 [[E 번호]] E641로 [[향미 (맛)|향미]] 증진제로 분류된다.<ref>{{서적 인용| vauthors = Winter R |title=A consumer's dictionary of food additives|date=2009|publisher=Three Rivers Press|location=New York|isbn=978-0307408921|edition=7th|url-access=registration|url=https://archive.org/details/isbn_9780307408921}}</ref>

=== 요구 사항 ===
미국 의학 연구소의 식품 영양 위원회(FNB)는 2002년에 [[필수 아미노산]]에 대한 권장 식이 허용량(RDA)을 제정했다. 19세 이상의 성인의 경우 매일 체중 1 kg당 42 mg의 류신이 필요하다.<ref name="DRItext">{{서적 인용|title=Dietary Reference Intakes for Energy, Carbohydrates, Fiber, Fat, Fatty Acids, Cholesterol, Protein, and Amino Acids|last1=Institute of Medicine|author1-link=|year=2002|publisher=The National Academies Press|location=Washington, DC|pages=589–768|chapter=Protein and Amino Acids|doi=10.17226/10490|isbn=978-0-309-08525-0|chapter-url=https://www.nap.edu/read/10490/chapter/12}}</ref>

=== 공급원 ===
{|class="wikitable"
|+ 류신의 식품 공급원<ref>{{서적 인용|title=National Nutrient Database for Standard Reference |url=http://www.nal.usda.gov/fnic/foodcomp/search/ |publisher=U.S. Department of Agriculture |access-date=16 September 2009 |url-status=dead |archive-url=https://web.archive.org/web/20150303184216/http://www.nal.usda.gov/fnic/foodcomp/search/ |archive-date= 3 March 2015 }}</ref>
|-
! 식품
! g/100g
|-
|농축 [[유청 단백질]], 건조 분말 || 10.0~12.0
|-
|농축 [[대두 단백질]], 건조 분말 || 7.5~8.5
|- 
|농축 [[완두 단백질]], 건조 분말 || 6.6
|-
|[[콩]], 성숙한 씨앗, 볶은 것, 소금에 절인 것 || 2.87
|-
|껍질을 벗긴 대마씨 || 2.16
|-
|[[쇠고기]], 원형, 상단 원형, 날것 || 1.76
|-
|[[땅콩]]|| 1.67
|-
|[[물고기]], 연어, 핑크, 날것 || 1.62
|-
|[[밀 배아]]|| 1.57
|-
|[[아몬드]]|| 1.49
|-
|[[닭고기]], 브로일러, 튀김용 닭, 넓적다리 고기, 날것 || 1.48
|-
|[[계란]], 노른자, 날것 || 1.40
|-
|[[귀리]]|| 1.28
|-
|[[풋콩]] (대두, 녹색, 날것) || 0.93
|-
| 콩, 핀토, 조리된 것 || 0.78
|-
|[[렌즈콩]], 조리된 것 ||  0.65
|-
|[[병아리콩]], 조리된 것 || 0.63
|-
|[[옥수수]], 노란색 || 0.35
|-
|[[우유]], 전유, 유지방 3.25% || 0.27
|-
|[[쌀]], 현미, 중간 곡물, 조리된 것 || 0.19
|-
|[[모유]]|| 0.10
|}

== 건강에 대한 효과 ==
[[식이 보충제]]로서 류신은 나이든 쥐의 근육 단백질의 합성을 증가시켜 근육 조직의 분해를 늦추는 것으로 밝혀졌다.<ref>{{저널 인용| vauthors = Combaret L, Dardevet D, Rieu I, Pouch MN, Béchet D, Taillandier D, Grizard J, Attaix D | display-authors = 6 | title = A leucine-supplemented diet restores the defective postprandial inhibition of proteasome-dependent proteolysis in aged rat skeletal muscle | journal = The Journal of Physiology | volume = 569 | issue = Pt 2 | pages = 489–99 | date = December 2005 | pmid = 16195315 | pmc = 1464228 | doi = 10.1113/jphysiol.2005.098004 | doi-access = free }}</ref> 그러나 비교 연구 결과는 상충된다. 장기간의 류신 보충은 건강한 노인 남성의 근육량이나 근력을 증가시키지 않는다.<ref>{{저널 인용| vauthors = Verhoeven S, Vanschoonbeek K, Verdijk LB, Koopman R, Wodzig WK, Dendale P, van Loon LJ | title = Long-term leucine supplementation does not increase muscle mass or strength in healthy elderly men | journal = The American Journal of Clinical Nutrition | volume = 89 | issue = 5 | pages = 1468–75 | date = May 2009 | pmid = 19321567 | doi = 10.3945/ajcn.2008.26668 | doi-access = free }}</ref> 더 많은 연구가 필요하며, 바람직하게는 객관적이고 무작위적인 사회 표본을 기반으로 하는 연구가 필요하다. 류신을 단독으로 또는 다른 [[가지사슬 아미노산]]과 함께 섭취하는 경우 류신 보충의 효과를 알아내기 위해 생활 방식, 연령, 성별, 식이, 운동 등과 같은 요인들을 분석시 고려해야 한다. 그때가지는 식이 류신 보충을 전체 인구에 대한 근육 생장 또는 최적 상태의 유지를 위한 주요 이유와 관련시킬 수 없다.

L-류신과 D-류신은 모두 [[뇌전증 발작]]으로부터 쥐를 보호한다.<ref name="pmid26054437">{{저널 인용| vauthors = Hartman AL, Santos P, O'Riordan KJ, Stafstrom CE, Marie Hardwick J | title = Potent anti-seizure effects of D-leucine | journal = Neurobiology of Disease | volume = 82 | pages = 46–53 | date = October 2015 | pmid = 26054437 | pmc = 4640989 | doi = 10.1016/j.nbd.2015.05.013 }}</ref> 또한 D-류신은 적어도 다이제팜만큼 효과적으로 진정 효과없이 발작이 시작된 후에 쥐의 발작을 종결시킨다.<ref name="pmid26054437"/> L-류신의 식이 섭취 감소는 쥐의 비만을 촉진한다.<ref>{{저널 인용| vauthors = Fontana L, Cummings NE, Arriola Apelo SI, Neuman JC, Kasza I, Schmidt BA, Cava E, Spelta F, Tosti V, Syed FA, Baar EL, Veronese N, Cottrell SE, Fenske RJ, Bertozzi B, Brar HK, Pietka T, Bullock AD, Figenshau RS, Andriole GL, Merrins MJ, Alexander CM, Kimple ME, Lamming DW | display-authors = 6 | title = Decreased Consumption of Branched-Chain Amino Acids Improves Metabolic Health | journal = Cell Reports | volume = 16 | issue = 2 | pages = 520–530 | date = July 2016 | pmid = 27346343 | pmc = 4947548 | doi = 10.1016/j.celrep.2016.05.092 }}</ref> 류신의 높은 혈중 수치는 사람, 쥐 및 설치류에서 인슐린 저항성과 관련이 있다.<ref>{{저널 인용| vauthors = Lynch CJ, Adams SH | title = Branched-chain amino acids in metabolic signalling and insulin resistance | journal = Nature Reviews. Endocrinology | volume = 10 | issue = 12 | pages = 723–36 | date = December 2014 | pmid = 25287287 | pmc = 4424797 | doi = 10.1038/nrendo.2014.171 }}</ref> 이것은 [[mTOR]] 신호전달을 자극하는 류신의 효과 때문일 수 있다.<ref>{{저널 인용| vauthors = Caron A, Richard D, Laplante M | title = The Roles of mTOR Complexes in Lipid Metabolism | journal = Annual Review of Nutrition | volume = 35 | pages = 321–48 | year = 2015 | pmid = 26185979 | doi = 10.1146/annurev-nutr-071714-034355 }}</ref> 류신 및 다른 가지사슬 아미노산의 식이 제한은 에너지 소비를 증가시켜 야행성 쥐에서 식이 유발 비만을 억제시킬 수 있고 과다섭취 쥐의 지방 증가를 제한할 수 있다.<ref>{{저널 인용| vauthors = Cummings NE, Williams EM, Kasza I, Konon EN, Schaid MD, Schmidt BA, Poudel C, Sherman DS, Yu D, Arriola Apelo SI, Cottrell SE, Geiger G, Barnes ME, Wisinski JA, Fenske RJ, Matkowskyj KA, Kimple ME, Alexander CM, Merrins MJ, Lamming DW | display-authors = 6 | title = Restoration of metabolic health by decreased consumption of branched-chain amino acids | journal = The Journal of Physiology | volume = 596 | issue = 4 | pages = 623–645 | date = February 2018 | pmid = 29266268 | pmc = 5813603 | doi = 10.1113/JP275075 }}</ref><ref>{{저널 인용| vauthors = White PJ, Lapworth AL, An J, Wang L, McGarrah RW, Stevens RD, Ilkayeva O, George T, Muehlbauer MJ, Bain JR, Trimmer JK, Brosnan MJ, Rolph TP, Newgard CB | display-authors = 6 | title = Branched-chain amino acid restriction in Zucker-fatty rats improves muscle insulin sensitivity by enhancing efficiency of fatty acid oxidation and acyl-glycine export | journal = Molecular Metabolism | volume = 5 | issue = 7 | pages = 538–551 | date = July 2016 | pmid = 27408778 | pmc = 4921791 | doi = 10.1016/j.molmet.2016.04.006 }}</ref>

== 안전성 ==
대상부전 [[단풍시럽뇨병]]에서 볼 수 있는 류신 독성은 [[섬망]]과 신경학적 손상을 유발하고 생명을 위협할 수 있다.<ref>{{저널 인용|last1=Yudkoff|first1=Marc|last2=Daikhin|first2=Yevgeny|last3=Nissim|first3=Ilana|last4=Horyn|first4=Oksana|last5=Luhovyy|first5=Bohdan|last6=Lazarow|first6=Adam|last7=Nissim|first7=Itzhak|date=2005-06-01|title=Brain Amino Acid Requirements and Toxicity: The Example of Leucine|url=https://academic.oup.com/jn/article/135/6/1531S/4663840|journal=The Journal of Nutrition|language=en|volume=135|issue=6|pages=1531S–1538S|doi=10.1093/jn/135.6.1531S|pmid=15930465|issn=0022-3166}}</ref>

류신을 많이 섭취하면 [[트립토판|L-트립토판]]이 니아신으로 전환되는 것을 방해하기 때문에 [[니아신]] 수치가 낮은 사람들에게 [[펠라그라]] 증상을 유발하거나 악화시킬 수 있다.<ref>{{저널 인용| vauthors = Badawy AA, Lake SL, Dougherty DM | title = Mechanisms of the pellagragenic effect of leucine: stimulation of hepatic tryptophan oxidation by administration of branched-chain amino acids to healthy human volunteers and the role of plasma free tryptophan and total kynurenines | journal = International Journal of Tryptophan Research | volume = 7 | pages = 23–32 | year = 2014 | pmid = 25520560 | pmc = 4259507 | doi = 10.4137/IJTR.S18231 }}</ref>

500 mg/kg/d를 초과하는 용량의 류신은 [[고암모니아혈증]]에서 관찰되었다.<ref name="pmid22952178">{{저널 인용| vauthors = Elango R, Chapman K, Rafii M, Ball RO, Pencharz PB | title = Determination of the tolerable upper intake level of leucine in acute dietary studies in young men | journal = The American Journal of Clinical Nutrition | volume = 96 | issue = 4 | pages = 759–67 | date = October 2012 | pmid = 22952178 | doi = 10.3945/ajcn.111.024471 | quote = A significant increase in blood ammonia concentrations above normal values, plasma leucine concentrations, and urinary leucine excretion were observed with leucine intakes >500 mg · kg<sup>−1</sup> · d<sup>−1</sup>. The oxidation of l-[1-<sup>13</sup>C]-leucine expressed as label tracer oxidation in breath (F<sup>13</sup>CO<sub>2</sub>), leucine oxidation, and α-ketoisocaproic acid (KIC) oxidation led to different results: a plateau in F<sup>13</sup>CO<sub>2</sub> observed after 500 mg · kg<sup>−1</sup> · d<sup>−1</sup>, no clear plateau observed in leucine oxidation, and KIC oxidation appearing to plateau after 750 mg · kg<sup>−1</sup> · d<sup>−1</sup>. On the basis of plasma and urinary variables, the UL for leucine in healthy adult men can be suggested at 500 mg · kg<sup>−1</sup> · d<sup>−1</sup> or ~35 g/d as a cautious estimate under acute dietary conditions. | doi-access = free }}</ref> 따라서 비공식적으로 건강한 성인 남성의 류신 허용 상한 섭취량(UL)은 급석 식이 조건에서 500 mg/kg/d 또는 35 g/d로 제안될 수 있다.<ref name="pmid22952178"/><ref name="pmid27138628">{{저널 인용| vauthors = Rasmussen B, Gilbert E, Turki A, Madden K, Elango R | title = Determination of the safety of leucine supplementation in healthy elderly men | journal = Amino Acids | volume = 48 | issue = 7 | pages = 1707–16 | date = July 2016 | pmid = 27138628 | doi = 10.1007/s00726-016-2241-0 | quote = the upper limit for leucine intake in healthy elderly could be set similar to young men at 500 mg kg-1 day-1 or ~35 g/day for an individual weighing 70 kg | s2cid = 3708265 }}</ref>

== 약리학 ==
=== 약력학 ===
류신은 [[근원섬유]] 근[[단백질 합성]]을 직접적으로 자극하는 능력을 가진 [[식이 (영양)|식이성]] [[아미노산]]이다.<ref>{{저널 인용| vauthors = Etzel MR | title = Manufacture and use of dairy protein fractions | journal = The Journal of Nutrition | volume = 134 | issue = 4 | pages = 996S–1002S | date = April 2004 | pmid = 15051860 | doi = 10.1093/jn/134.4.996S | doi-access = free }}</ref> 류신의 이러한 효과는 [[단백질 생합성]] 및 [[세포 생장]]을 조절하는 [[세린-트레오닌 단백질 키네이스]]인 [[mTOR]]의 활성인자로서의 역할에서 비롯된다.<ref name="Pharmacology of HMB-FA in humans in vivo" /> 류신에 의한 mTOR의 활성화는 Rag GTPase,<ref name="pmid28963468">{{저널 인용| vauthors = Kim JH, Lee C, Lee M, Wang H, Kim K, Park SJ, Yoon I, Jang J, Zhao H, Kim HK, Kwon NH, Jeong SJ, Yoo HC, Kim JH, Yang JS, Lee MY, Lee CW, Yun J, Oh SJ, Kang JS, Martinis SA, Hwang KY, Guo M, Han G, Han JM, Kim S | display-authors = 6 | title = Control of leucine-dependent mTORC1 pathway through chemical intervention of leucyl-tRNA synthetase and RagD interaction | journal = Nature Communications | volume = 8 | issue = 1 | pages = 732 | date = September 2017 | pmid = 28963468 | pmc = 5622079 | doi = 10.1038/s41467-017-00785-0 | bibcode = 2017NatCo...8..732K }}</ref><ref name="pmid23361334">{{저널 인용| vauthors = Jewell JL, Russell RC, Guan KL | title = Amino acid signalling upstream of mTOR | journal = Nature Reviews. Molecular Cell Biology | volume = 14 | issue = 3 | pages = 133–9 | date = March 2013 | pmid = 23361334 | pmc = 3988467 | doi = 10.1038/nrm3522 }}</ref><ref name="pmid18497260">{{저널 인용| vauthors = Sancak Y, Peterson TR, Shaul YD, Lindquist RA, Thoreen CC, Bar-Peled L, Sabatini DM | title = The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1 | journal = Science | volume = 320 | issue = 5882 | pages = 1496–501 | date = June 2008 | pmid = 18497260 | pmc = 2475333 | doi = 10.1126/science.1157535 | bibcode = 2008Sci...320.1496S }}</ref> [[류실-tRNA 합성효소]]에 대한 류신의 결합,<ref name="pmid28963468" /><ref name="pmid23361334" /> [[세스트린 2]]에 대한 류신의 결합,<ref>{{저널 인용| vauthors = Wolfson RL, Chantranupong L, Saxton RA, Shen K, Scaria SM, Cantor JR, Sabatini DM | title = Sestrin2 is a leucine sensor for the mTORC1 pathway | journal = Science | volume = 351 | issue = 6268 | pages = 43–8 | date = January 2016 | pmid = 26449471 | pmc = 4698017 | doi = 10.1126/science.aab2674 | bibcode = 2016Sci...351...43W }}</ref><ref>{{저널 인용| vauthors = Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM | display-authors = 6 | title = Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway | journal = Science | volume = 351 | issue = 6268 | pages = 53–8 | date = January 2016 | pmid = 26586190 | pmc = 4698039 | doi = 10.1126/science.aad2087 | bibcode = 2016Sci...351...53S }}</ref><ref>{{저널 인용| vauthors = Chantranupong L, Wolfson RL, Orozco JM, Saxton RA, Scaria SM, Bar-Peled L, Spooner E, Isasa M, Gygi SP, Sabatini DM | display-authors = 6 | title = The Sestrins interact with GATOR2 to negatively regulate the amino-acid-sensing pathway upstream of mTORC1 | journal = Cell Reports | volume = 9 | issue = 1 | pages = 1–8 | date = October 2014 | pmid = 25263562 | pmc = 4223866 | doi = 10.1016/j.celrep.2014.09.014 }}</ref> 및 다른 가능한 메커니즘을 통해 매개된다.

=== 사람에서의 물질대사 ===
[[파일:HMB biosynthesis and metabolism.png|섬네일|600px|오른쪽|사람에서 [[류신|L-류신]]과 관련한 [[β-하이드록시 β-메틸뷰티르산]](HMB) 및 아이소발레릴-CoA에 대한 [[대사 경로]]. 두 가지 주요 경로 중 L-류신은 대부분 아이소발레릴-CoA로 대사되는 반면, β-하이드록시 β-메틸뷰티르산(HMB)으로 대사되는 경우는 약 5%에 불과하다.<ref>{{저널 인용| vauthors = Wilson JM, Fitschen PJ, Campbell B, Wilson GJ, Zanchi N, Taylor L, Wilborn C, Kalman DS, Stout JR, Hoffman JR, Ziegenfuss TN, Lopez HL, Kreider RB, Smith-Ryan AE, Antonio J | title = International Society of Sports Nutrition Position Stand: beta-hydroxy-beta-methylbutyrate (HMB) | journal = Journal of the International Society of Sports Nutrition | volume = 10 | issue = 1 | pages = 6 | date = February 2013 | pmid = 23374455 | pmc = 3568064 | doi = 10.1186/1550-2783-10-6}}</ref><ref>{{저널 인용| vauthors = Zanchi NE, Gerlinger-Romero F, Guimarães-Ferreira L, de Siqueira Filho MA, Felitti V, Lira FS, Seelaender M, Lancha AH | title = HMB supplementation: clinical and athletic performance-related effects and mechanisms of action | journal = Amino Acids | volume = 40 | issue = 4 | pages = 1015–1025 | date = April 2011 | pmid = 20607321 | doi = 10.1007/s00726-010-0678-0 | quote = HMB is a metabolite of the amino acid leucine (Van Koverin and Nissen 1992), an essential amino acid. The first step in HMB metabolism is the reversible transamination of leucine to [α-KIC] that occurs mainly extrahepatically (Block and Buse 1990). Following this enzymatic reaction, [α-KIC] may follow one of two pathways. In the first, HMB is produced from [α-KIC] by the cytosolic enzyme KIC dioxygenase (Sabourin and Bieber 1983). The cytosolic dioxygenase has been characterized extensively and differs from the mitochondrial form in that the dioxygenase enzyme is a cytosolic enzyme, whereas the dehydrogenase enzyme is found exclusively in the mitochondrion (Sabourin and Bieber 1981, 1983). Importantly, this route of HMB formation is direct and completely dependent of liver KIC dioxygenase. Following this pathway, HMB in the cytosol is first converted to cytosolic β-hydroxy-β-methylglutaryl-CoA (HMG-CoA), which can then be directed for cholesterol synthesis (Rudney 1957) (Fig. 1). In fact, numerous biochemical studies have shown that HMB is a precursor of cholesterol (Zabin and Bloch 1951; Nissen et al. 2000).<!--<br /><br /> In the second pathway, after transamination, [α-KIC] in liver generates isovaleryl-CoA through the enzymatic action of branched-chain ketoacid dehydrogenase (BCKD) and after several steps, there is production of HMG-CoA through the enzyme HMG-CoA synthase (Fig. 1). Under normal conditions the majority of KIC is converted into isovaleryl-CoA, in which approximately 5% of leucine is metabolized into HMB (Wilson et al. 2008; Van Koverin and Nissen 1992). However, Nissen and Abumrad (1997) provided evidence that the primary fate of HMB is probably conversion to HMG-CoA in the liver, for cholesterol biosynthesis.--> }}</ref><ref>{{서적 인용| vauthors=Kohlmeier M | title=Nutrient Metabolism: Structures, Functions, and Genes | date=May 2015 | publisher=Academic Press | isbn=978-0-12-387784-0 | pages=385–388 | edition=2nd | section-url=https://books.google.com/books?id=aTQTAAAAQBAJ&pg=PA387&q=beta-hydroxy%20beta-methylbutyrate%20HMB#v=onepage | url=https://books.google.com/books?id=aTQTAAAAQBAJ&printsec=frontcover#v=onepage | accessdate=6 June 2016 | section=Leucine | quote= Energy fuel: Eventually, most Leu is broken down, providing about 6.0kcal/g. About 60% of ingested Leu is oxidized within a few hours&nbsp;... Ketogenesis: A significant proportion (40% of an ingested dose) is converted into acetyl-CoA and thereby contributes to the synthesis of ketones, steroids, fatty acids, and other compounds}}<br />[https://books.google.com/books?id=aTQTAAAAQBAJ&pg=PA386#v=onepage&q&f=false Figure 8.57: Metabolism of {{smallcaps all|L}}-leucine]</ref>]]

류신 대사는 인체의 많은 [[조직 (생물학)|조직]]에서 일어난다. 그러나 대부분의 식이 류신은 [[간]], [[지방 조직]] 및 [[근육 조직]] 내에서 대사된다.<ref name="pmid4855772"/> 지방 조직 및 근육 조직은 [[스테롤]] 및 기타 화합물의 형성에 류신을 사용한다.<ref name="pmid4855772"/> 이들 두 조직에서 결합된 류신의 사용은 간보다 7배 더 많다.<ref name="pmid4855772">{{저널 인용| vauthors = Rosenthal J, Angel A, Farkas J | title = Metabolic fate of leucine: a significant sterol precursor in adipose tissue and muscle | journal = The American Journal of Physiology | volume = 226 | issue = 2 | pages = 411–8 | date = February 1974 | pmid = 4855772 | doi = 10.1152/ajplegacy.1974.226.2.411 | doi-access = free }}</ref>

건강한 사람의 경우 식이 L-류신의 약 60%가 몇 시간 후에 대사되고, 식이 L-류신의 약 5%(2~10% 범위)가 [[β-하이드록시 β-메틸뷰티르산]](HMB)으로 전환된다.<ref name="HMB athletic performance-related effects 2011 review" /><ref name="Molecular Aspects of Medicine 2016 review">{{저널 인용|vauthors=Brioche T, Pagano AF, Py G, Chopard A|date=August 2016|title=Muscle wasting and aging: Experimental models, fatty infiltrations, and prevention|url=https://hal.archives-ouvertes.fr/hal-01837630/file/2016_Brioche_MAM_1.pdf|journal=Molecular Aspects of Medicine|volume=50|pages=56–87|doi=10.1016/j.mam.2016.04.006|pmid=27106402|quote=<!--HMB can decrease apoptosis, judging by a dramatic decrease in the number of TUNEL-positive nuclei in the soleus and plantaris of hindlimb-unloaded old rats treated with HMB, as compared to a placebo group.&nbsp;... Similar data were obtained in muscle cell cultures (Kornasio et al., 2009).&nbsp;...--> In conclusion, HMB treatment clearly appears to be a safe potent strategy against sarcopenia, and more generally against muscle wasting, because HMB improves muscle mass, muscle strength, and physical performance. It seems that HMB is able to act on three of the four major mechanisms involved in muscle deconditioning (protein turnover, apoptosis, and the regenerative process), whereas it is hypothesized to strongly affect the fourth (mitochondrial dynamics and functions). Moreover, HMB is inexpensive (~30– 50 US dollars per month at 3 g per day) and may prevent osteopenia (Bruckbauer and Zemel, 2013; Tatara, 2009; Tatara et al., 2007, 2008, 2012) and decrease cardiovascular risks (Nissen et al., 2000). For all these reasons, HMB should be routinely used in muscle-wasting conditions especially in aged people.&nbsp;... 3&nbsp;g of CaHMB taken three times a day (1&nbsp;g each time) is the optimal posology, which allows for continual bioavailability of HMB in the body (Wilson et al., 2013)}}</ref><ref name="Leucine metabolism" /> 식이 L-류신의 약 40%는 아세틸-CoA로 전환되며, 이는 이후에 다른 화합물의 합성에 사용된다.<ref name="Leucine metabolism" />

대부분의 L-류신 대사는 초기에 [[가지사슬 아미노산 아미노기전이효소]]에 의해 촉매되어 [[α-케토아이소카프로산]](α-KIC)을 생성한다.<ref name="HMB athletic performance-related effects 2011 review">{{저널 인용| vauthors = Zanchi NE, Gerlinger-Romero F, Guimarães-Ferreira L, de Siqueira Filho MA, Felitti V, Lira FS, Seelaender M, Lancha AH | title = HMB supplementation: clinical and athletic performance-related effects and mechanisms of action | journal = Amino Acids | volume = 40 | issue = 4 | pages = 1015–1025 | date = April 2011 | pmid = 20607321 | doi = 10.1007/s00726-010-0678-0 | s2cid = 11120110 | url = https://repositorio.unal.edu.co/handle/unal/77957 | quote = HMB is a metabolite of the amino acid leucine (Van Koverin and Nissen 1992), an essential amino acid. The first step in HMB metabolism is the reversible transamination of leucine to [α-KIC] that occurs mainly extrahepatically (Block and Buse 1990). Following this enzymatic reaction, [α-KIC] may follow one of two pathways. In the first, HMB is produced from [α-KIC] by the cytosolic enzyme KIC dioxygenase (Sabourin and Bieber 1983). The cytosolic dioxygenase has been characterized extensively and differs from the mitochondrial form in that the dioxygenase enzyme is a cytosolic enzyme, whereas the dehydrogenase enzyme is found exclusively in the mitochondrion (Sabourin and Bieber 1981, 1983). Importantly, this route of HMB formation is direct and completely dependent of liver KIC dioxygenase. Following this pathway, HMB in the cytosol is first converted to cytosolic β-hydroxy-β-methylglutaryl-CoA (HMG-CoA), which can then be directed for cholesterol synthesis (Rudney 1957) (Fig. 1). In fact, numerous biochemical studies have shown that HMB is a precursor of cholesterol (Zabin and Bloch 1951; Nissen et al. 2000).<!--<br /><br /> In the second pathway, after transamination, [α-KIC] in liver generates isovaleryl-CoA through the enzymatic action of branched-chain ketoacid dehydrogenase (BCKD) and after several steps, there is production of HMG-CoA through the enzyme HMG-CoA synthase (Fig. 1). Under normal conditions the majority of KIC is converted into isovaleryl-CoA, in which approximately 5% of leucine is metabolized into HMB (Wilson et al. 2008; Van Koverin and Nissen 1992). However, Nissen and Abumrad (1997) provided evidence that the primary fate of HMB is probably conversion to HMG-CoA in the liver, for cholesterol biosynthesis.--> }}</ref><ref name="Leucine metabolism">{{서적 인용| vauthors=Kohlmeier M | title=Nutrient Metabolism: Structures, Functions, and Genes | date=May 2015 | publisher=Academic Press | isbn=978-0-12-387784-0 | pages=385–388 | edition=2nd | section-url=https://books.google.com/books?id=aTQTAAAAQBAJ&q=beta-hydroxy%20beta-methylbutyrate%20HMB&pg=PA387 | url=https://books.google.com/books?id=aTQTAAAAQBAJ | access-date=6 June 2016 | section=Leucine | quote=Energy fuel: Eventually, most Leu is broken down, providing about 6.0kcal/g. About 60% of ingested Leu is oxidized within a few hours&nbsp;... Ketogenesis: A significant proportion (40% of an ingested dose) is converted into acetyl-CoA and thereby contributes to the synthesis of ketones, steroids, fatty acids, and other compounds | url-status=live | archive-url=https://web.archive.org/web/20180322000056/https://books.google.com/books?id=aTQTAAAAQBAJ&printsec=frontcover#v=onepage | archive-date=22 March 2018}}<br />[https://books.google.com/books?id=aTQTAAAAQBAJ&pg=PA386#v=onepage Figure 8.57: Metabolism of {{smallcaps all|L}}-leucine] {{webarchive|url=https://web.archive.org/web/20180322000056/https://books.google.com/books?id=aTQTAAAAQBAJ&pg=PA386 |date=22 March 2018 }}</ref> α-케토아이소카프로산은 대부분 [[미토콘드리아]]의 효소인 [[가지사슬 α-케토산 탈수소효소 복합체]]에 의해 대사되어 [[아이소발레릴-CoA]]로 전환된다.<ref name="HMB athletic performance-related effects 2011 review" /><ref name="Leucine metabolism" /> 아이소발레릴-CoA는 이후에 [[아이소발레릴-CoA 탈수소효소]]에 의해 대사되어 아세틸-CoA 및 기타 화합물의 합성에 사용되는 [[β-메틸크로토닐-CoA]]로 전환된다.<ref name="Leucine metabolism" /> [[비오틴 결핍증]]에서 β-하이드록시 β-메틸뷰티르산(HMB)은 β-메틸크로토닐-CoA(MC-CoA)를 [[β-하이드록시 β-메틸뷰티릴-CoA]](HMB-CoA)로, β-하이드록시 β-메틸뷰티릴-CoA를 β-하이드록시 β-메틸뷰티르산으로 각각 전환시키는<ref name="pmid21918059">{{저널 인용|title=Urinary excretion of 3-hydroxyisovaleric acid and 3-hydroxyisovaleryl carnitine increases in response to a leucine challenge in marginally biotin-deficient humans|journal=The Journal of Nutrition|date=November 2011|volume=141|issue=11|pages=1925–1930|doi=10.3945/jn.111.146126|pmc=3192457|pmid=21918059|quote=Reduced activity of MCC impairs catalysis of an essential step in the mitochondrial catabolism of the BCAA leucine. Metabolic impairment diverts methylcrotonyl CoA to 3-hydroxyisovaleryl CoA in a reaction catalyzed by enoyl-CoA hydratase (22, 23). 3-Hydroxyisovaleryl CoA accumulation can inhibit cellular respiration either directly or via effects on the ratios of acyl CoA:free CoA if further metabolism and detoxification of 3-hydroxyisovaleryl CoA does not occur (22). The transfer to carnitine by 4 carnitine acyl-CoA transferases distributed in subcellular compartments likely serves as an important reservoir for acyl moieties (39–41). 3-Hydroxyisovaleryl CoA is likely detoxified by carnitine acetyltransferase producing 3HIA-carnitine, which is transported across the inner mitochondrial membrane (and hence effectively out of the mitochondria) via carnitine-acylcarnitine translocase (39). 3HIA-carnitine is thought to be either directly deacylated by a hydrolase to 3HIA or to undergo a second CoA exchange to again form 3-hydroxyisovaleryl CoA followed by release of 3HIA and free CoA by a thioesterase.|vauthors=Mock DM, Stratton SL, Horvath TD, Bogusiewicz A, Matthews NI, Henrich CL, Dawson AM, Spencer HJ, Owen SN, Boysen G, Moran JH|department=primary source}}</ref> [[엔오일-CoA 수화효소]]와 알려지지 않은 [[싸이오에스터레이스]]를 통해 β-메틸크로토닐-CoA로부터 합성될 수 있다.<ref name="HMB-CoA ⇔ HMB">{{웹 인용|title=KEGG Reaction: R10759|url=http://www.genome.jp/dbget-bin/www_bget?rn:R10759|website=Kyoto Encyclopedia of Genes and Genomes|publisher=Kanehisa Laboratories|access-date=24 June 2016|url-status=live|archive-url=https://web.archive.org/web/20160701140720/http://www.genome.jp/dbget-bin/www_bget?rn:R10759|archive-date=1 July 2016}}</ref><ref name="pmid21918059" /><ref name="HMB-CoA ⇔ MC-CoA">{{웹 인용|title=KEGG Reaction: R04137|url=http://www.genome.jp/dbget-bin/www_bget?rn:R04137|website=Kyoto Encyclopedia of Genes and Genomes|publisher=Kanehisa Laboratories|access-date=24 June 2016|url-status=live|archive-url=https://web.archive.org/web/20160701144143/http://www.genome.jp/dbget-bin/www_bget?rn:R04137|archive-date=1 July 2016}}</ref> 상대적으로 적은 양의 α-케토아이소카프로산은 [[세포질]]의 [[효소]] [[4-하이드록시페닐피루브산 이산소화효소]]에 의해 [[간]]에서 β-하이드록시 β-메틸뷰티르산으로 전환된다.<ref name="HMB athletic performance-related effects 2011 review" /><ref name="Leucine metabolism" /><ref name="KIC dioxygenase">{{웹 인용|title=Homo sapiens: 4-hydroxyphenylpyruvate dioxygenase reaction|url=http://www.biocyc.org/META/NEW-IMAGE?type=REACTION&object=RXN-13640|website=MetaCyc|publisher=SRI International|access-date=6 June 2016|date=20 August 2012}}</ref> 건강한 사람의 경우 L-류신이 α-케토아이소카프로산으로 전환된 다음 β-하이드록시 β-메틸뷰티르산으로 전환되는 이러한 마이너 경로가 β-하이드록시 β-메틸뷰티르산 합성의 주요 경로이다.<ref name="HMB athletic performance-related effects 2011 review" /><ref name="Leucine metabolism" />

L-류신 대사의 작은 부분(약 33%를 차지하는 [[고환]]을 제외한 모든 조직에서 5% 미만)은 초기에 [[류신 2,3-아미노뮤테이스]]에 의해 촉매되어 [[β-류신]]을 생성하고, 이는 후속적으로 일련의 특성화되지 않은 효소들에 의해 [[β-케토아이소카프로산]], β-케토아이소카프로일-CoA, [[아세틸-CoA]]로 대사된다.<ref name="Leucine metabolism" /><ref name="BRENDA leucine metabolism" />

β-하이드록시 β-메틸뷰티르산(HMB)의 대사는 [[β-하이드록시 β-메틸뷰티릴-CoA]](HMB-CoA)로 전환시키는 특성화되지 않은 효소에 의해 촉매된다.<ref name="HMB-CoA ⇔ HMB"/><ref name="Leucine metabolism" /> β-하이드록시 β-메틸뷰티릴-CoA는 [[엔오일-CoA 수화효소]] 또는 다른 특성화되지 않은 효소에 의해 대사되어 각각 [[β-메틸크로토닐-CoA]](MC-CoA) 또는 [[β-하이드록시 β-메틸글루타릴-CoA]](HMG-CoA)를 생성한다.<ref name="HMB athletic performance-related effects 2011 review" /><ref name="Leucine metabolism" /> 그런 다음 β-메틸크로토닐-CoA는 [[메틸크로토닐-CoA 카복실화효소]]에 의해 [[β-메틸글루타코닐-CoA]](MG-CoA)로 전환되고, 이는 후속적으로 [[메틸글루타코닐-CoA 수화효소]]에 의해 β-하이드록시 β-메틸글루타릴-CoA로 전환된다.<ref name="HMB athletic performance-related effects 2011 review" /><ref name="Leucine metabolism" /><ref name="BRENDA leucine metabolism">{{웹 인용|title=Leucine metabolism|url=http://www.brenda-enzymes.org/pathways/Maps/pathways/leucine_metabolism.svg|website=BRENDA|publisher=Technische Universität Braunschweig|access-date=12 August 2016|url-status=dead|archive-url=https://web.archive.org/web/20160817213425/http://www.brenda-enzymes.org/pathways/Maps/pathways/leucine_metabolism.svg|archive-date=17 August 2016}}</ref> 그런 다음 β-하이드록시 β-메틸글루타릴-CoA는 [[β-하이드록시 β-메틸글루타릴-CoA 분해효소]]에 의해 [[아세틸-CoA]]와 [[아세토아세트산]]으로 분해되거나 [[메발론산 경로]]를 통해 [[콜레스테롤]]의 생산에 사용된다.<ref name="HMB athletic performance-related effects 2011 review" /><ref name="Leucine metabolism" />

== 사람 이외의 생물에서의 합성 ==
[[동물]]에서 류신은 잠재적인 [[전구체]] 화합물로부터 [[신생합성]]되는 완전한 [[대사 경로]]가 없기 때문에 동물의 식단에서 [[필수 아미노산]]이다. 따라서 동물은 일반적으로 [[단백질]]의 구성 성분으로 류신을 섭취해야 한다. [[식물]]과 [[미생물]]은 일련의 [[효소]]들을 사용하여 [[피루브산]]으로부터 류신을 합성한다.<ref>{{서적 인용| vauthors = Lehninger AL, Nelson DL, Cox MM |title=Lehninger principles of biochemistry. |date=2000 |publisher=Worth Publishers |location=New York |isbn=978-1-57259-153-0 |edition=3rd}}</ref>
* [[아세토락트산 생성효소]]
* [[아세토하이드록시산 아이소머로리덕테이스]]
* [[다이하이드록시산 탈수효소]]
* α-아이소프로필말산 생성효소
* α-아이소프로필말산 이성질화효소
* 류신 아미노기전이효소
소수성 아미노산인 [[발린]]의 합성에도 이 대사 경로의 초기 부분이 사용된다.

== 화학 ==
[[파일:Betain-Leucin.png|섬네일|오른쪽|350px|왼쪽은 (''S'')-류신(또는 L-류신), 오른쪽은 (''R'')-류신(또는 D-류신), 중성 pH에서 양쪽성 이온의 형태]]
류신은 선형이 아닌 [[지방족 화합물|지방족]] [[곁사슬]]을 가지고 있기 때문에 [[가지사슬 아미노산]]이다.

[[라세미 혼합물|라세미]] 류신은 [[생체분자]]의 비대칭 기원을 더 잘 이해하기 위해 원형 [[편광]] [[싱크로트론 방사]]에 노출되었다. 2.6%의 거울성 이성질체의 증가가 유도되었으며, 이는 생체분자의 [[호모카이랄성]]의 가능한 광화학적 기원을 나타낸다.<ref>Meierhenrich: ''Amino acids and the asymmetry of life'', Springer-Verlag, 2008, {{ISBN|978-3-540-76885-2}}.</ref>

== 같이 보기 ==
* [[아이소류신]]
* [[발린]]
* [[가지사슬 아미노산]]
* [[류신류]] – 류신의 이성질체 및 유도체
* [[류신 지퍼]] – 전사인자 단백질의 공통적인 모티프

== 각주 ==
{{각주|30em}}

== 외부 링크 ==
* {{두피디아|101013000709906}}
* [http://www.chem.qmul.ac.uk/iubmb/enzyme/reaction/AminoAcid/Leu.html 류신 생합성 (영어)]

{{아미노산}}
{{아미노산 대사 중간생성물들}}

[[분류:단백질성 아미노산]]
[[분류:케톤체 생성성 아미노산]]
[[분류:가지사슬 아미노산]]
[[분류:필수 아미노산]]
[[분류:E 번호 첨가제]]