Question: which site of an enzyme is called allosteric site
[{'answer': 'regulatory site', 'provenance': [{'wikipedia_id': '106256', 'title': 'Allosteric regulation', 'start_paragraph_id': 2, 'start_character': 73, 'end_paragraph_id': 2, 'end_character': 88, 'bleu_score': 1.0, 'section': 'Section::::Abstract.'}]}, {'provenance': [{'wikipedia_id': '188688', 'title': 'Active site', 'section': 'Section::::Abstract.', 'start_paragraph_id': 1, 'end_paragraph_id': 1, 'meta': {'evidence_span': ['In biology, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of residues that form temporary bonds with the substrate (binding site) and residues that catalyse a reaction of that substrate (catalytic site). Although the active site is small relative to the whole volume of the enzyme (it only occupies 10~20% of the total volume), it is the most important part of the enzyme as it directly catalyzes the chemical reaction. It usually consists of three to four amino acids, while other amino acids within the protein are required to maintain the protein tertiary structure of the enzyme.', 'In biology, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of residues that form temporary bonds with the substrate (binding site) and residues that catalyse a reaction of that substrate (catalytic site). Although the active site is small relative to the whole volume of the enzyme (it only occupies 10~20% of the total volume), it is the most important part of the enzyme as it directly catalyzes the chemical reaction. It usually consists of three to four amino acids, while other amino acids within the protein are required to maintain the protein tertiary structure of the enzyme.']}}]}, {'provenance': [{'wikipedia_id': '188688', 'title': 'Active site', 'section': 'Section::::Abstract.', 'start_paragraph_id': 2, 'end_paragraph_id': 2, 'meta': {'evidence_span': ['three to four amino acids, while other amino acids within the protein are required to maintain the protein tertiary structure of the enzyme. Each active site is evolved to be optimised to bind a particular substrate and catalyse a particular reaction, resulting in high specificity. This specificity is determined by the arrangement of amino acids within the active site and the structure of the substrates. Sometimes enzymes also need to bind with some cofactors to fulfil their function. The active site is usually a groove or pocket of the enzyme which can be located in a deep tunnel within the enzyme, or between the interfaces of multimeric enzymes. An active site can catalyse a reaction repeatedly as residues are not altered at the end of the reaction (they may change during the reaction, but are regenerated by the end). This process is achieved by lowering the activation energy of the reaction, so more substrates have enough energy to undergo reaction.', 'three to four amino acids, while other amino acids within the protein are required to maintain the protein tertiary structure of the enzyme. Each active site is evolved to be optimised to bind a particular substrate and catalyse a particular reaction, resulting in high specificity. This specificity is determined by the arrangement of amino acids within the active site and the structure of the substrates. Sometimes enzymes also need to bind with some cofactors to fulfil their function. The active site is usually a groove or pocket of the enzyme which can be located in a deep tunnel within the enzyme, or between the interfaces of multimeric enzymes. An active site can catalyse a reaction repeatedly as residues are not altered at the end of the reaction (they may change during the reaction, but are regenerated by the end). This process is achieved by lowering the activation energy of the reaction, so more substrates have enough energy to undergo reaction.']}}]}, {'provenance': [{'wikipedia_id': '106256', 'title': 'Allosteric regulation', 'section': 'Section::::Abstract.', 'start_paragraph_id': 2, 'end_paragraph_id': 2, 'meta': {'evidence_span': ['The site to which the effector binds is termed the "allosteric site" or "regulatory site".', 'The site to which the effector binds is termed the "allosteric site" or "regulatory site". Allosteric sites allow effectors to bind to the protein, often resulting in a conformational change involving protein dynamics. Effectors that enhance the protein\'s activity are referred to as "allosteric activators", whereas those that decrease the protein\'s activity are called "allosteric inhibitors".', 'The site to which the effector binds is termed the "allosteric site" or "regulatory site". Allosteric sites allow effectors to bind to the protein, often resulting in a conformational change involving protein dynamics. Effectors that enhance the protein\'s activity are referred to as "allosteric activators", whereas those that decrease the protein\'s activity are called "allosteric inhibitors".']}}]}, {'provenance': [{'wikipedia_id': '30351926', 'title': 'ASD (database)', 'section': 'Section::::Abstract.', 'start_paragraph_id': 1, 'end_paragraph_id': 1, 'meta': {'evidence_span': ['Allostery is the most direct and efficient way for regulation of biological macromolecule function induced by the binding of a ligand at an allosteric site topographically distinct from the orthosteric site. Due to the inherent high receptor selectivity and lower target-based toxicity, it is also expected to play a more positive role in drug discovery and bioengineering, leading to rapid growth on allosteric findings.', 'Allostery is the most direct and efficient way for regulation of biological macromolecule function induced by the binding of a ligand at an allosteric site topographically distinct from the orthosteric site. Due to the inherent high receptor selectivity and lower target-based toxicity, it is also expected to play a more positive role in drug discovery and bioengineering, leading to rapid growth on allosteric findings.']}}]}]