پیرووات دهیدروژناز (لیپوآمید)
بیشتر بخوانید

Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS (Jun 2003). "Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase". The Journal of Biological Chemistry. 278 (23): 21240–6. doi:10.1074/jbc.M300339200. PMID 12651851.
Okajima K, Korotchkina LG, Prasad C, Rupar T, Phillips JA, Ficicioglu C, Hertecant J, Patel MS, Kerr DS (Apr 2008). "Mutations of the E1beta subunit gene (PDHB) in four families with pyruvate dehydrogenase deficiency". Molecular Genetics and Metabolism. 93 (4): 371–80. doi:10.1016/j.ymgme.2007.10.135. PMID 18164639.
Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
Brown RM, Head RA, Boubriak II, Leonard JV, Thomas NH, Brown GK (Jul 2004). "Mutations in the gene for the E1beta subunit: a novel cause of pyruvate dehydrogenase deficiency". Human Genetics. 115 (2): 123–7. doi:10.1007/s00439-004-1124-8. PMID 15138885.
Sugden MC, Holness MJ (May 2003). "Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs". American Journal of Physiology. Endocrinology and Metabolism. 284 (5): E855–62. doi:10.1152/ajpendo.00526.2002. PMID 12676647.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Korotchkina LG, Patel MS (Feb 2008). "Binding of pyruvate dehydrogenase to the core of the human pyruvate dehydrogenase complex". FEBS Letters. 582 (3): 468–72. doi:10.1016/j.febslet.2007.12.041. PMC 2262399. PMID 18206651.
Fang R, Nixon PF, Duggleby RG (Oct 1998). "Identification of the catalytic glutamate in the E1 component of human pyruvate dehydrogenase". FEBS Letters. 437 (3): 273–7. doi:10.1016/S0014-5793(98)01249-6. PMID 9824306.
Han Z, Zhong L, Srivastava A, Stacpoole PW (Jan 2008). "Pyruvate dehydrogenase complex deficiency caused by ubiquitination and proteasome-mediated degradation of the E1 subunit". The Journal of Biological Chemistry. 283 (1): 237–43. doi:10.1074/jbc.M704748200. PMID 17923481.
Caruso M, Maitan MA, Bifulco G, Miele C, Vigliotta G, Oriente F, Formisano P, Beguinot F (Nov 2001). "Activation and mitochondrial translocation of protein kinase Cdelta are necessary for insulin stimulation of pyruvate dehydrogenase complex activity in muscle and liver cells". The Journal of Biological Chemistry. 276 (48): 45088–97. doi:10.1074/jbc.M105451200. PMID 11577086.
Hirner S, Krohne C, Schuster A, Hoffmann S, Witt S, Erber R, Sticht C, Gasch A, Labeit S, Labeit D (Jun 2008). "MuRF1-dependent regulation of systemic carbohydrate metabolism as revealed from transgenic mouse studies". Journal of Molecular Biology. 379 (4): 666–77. doi:10.1016/j.jmb.2008.03.049. PMID 18468620.
Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S (Jan 2006). "The LIFEdb database in 2006". Nucleic Acids Research. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
Hiromasa Y, Fujisawa T, Aso Y, Roche TE (Feb 2004). "Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components". The Journal of Biological Chemistry. 279 (8): 6921–33. doi:10.1074/jbc.M308172200. PMID 14638692.
Hartley JL, Temple GF, Brasch MA (Nov 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A (Oct 2004). "From ORFeome to biology: a functional genomics pipeline". Genome Research. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
| ن ب ونگارخانه PDB | ن ب ونگارخانه PDB |
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 3exi: Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex with the subunit-binding domain (SBD) of E2p, but SBD cannot be modeled into the electron density  3exe: Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex  3exf: Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex  1ni4: HUMAN PYRUVATE DEHYDROGENASE  3exg: Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex  3exh: Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex  2ozl: Human pyruvate dehydrogenase S264E variant :  3exi: Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex with the subunit-binding domain (SBD) of E2p, but SBD cannot be modeled into the electron density  3exe: Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex  3exf: Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex  1ni4: HUMAN PYRUVATE DEHYDROGENASE  3exg: Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex  3exh: Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex  2ozl: Human pyruvate dehydrogenase S264E variant 
| ن ب وآنزیم‌ها | ن ب وآنزیم‌ها |
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فعالیت:  جایگاه فعال  جایگاه اتصال  سه‌گانه کاتالیزگر  Oxyanion hole  Enzyme promiscuity  Catalytically perfect enzyme  کوآنزیم  کوفاکتور  کاتالیز آنزیم 
قواعد:  دگرریختاری  Cooperativity  بازدارنده آنزیم  فعال‌کننده آنزیم 
دسته‌بندی:  عدد گروه آنزیم  ابرخانواده آنزیم  خانواده آنزیم  فهرست آنزیم‌ها 
سینتیک:  سینتیک میکائلیس–منتن  طرح ادی هوفستی  طرح لاینویور برک  طرح هانس وولف 
انواع:  ای‌سی۱ اکسیدوردوکتازها (فهرست)  ای‌سی۲ ترانسفرازها (فهرست)  ای‌سی۳ هیدرولازها (فهرست)  ای‌سی۴ لیازها (فهرست)  ای‌سی۵ ایزومرازها (فهرست)  ای‌سی۶ لیگازها (فهرست)  ای‌سی۷ ترنسلوکازها (فهرست)