001package org.biopax.paxtools.model.level3; 002 003 004/** 005 * Defines the nature of the control relationship between the controller and the controlled entities. 006*/ 007public enum ControlType 008{ 009 /** 010 * General activation. Compounds that activate the specified enzyme activity by an unknown mechanism. The 011 * mechanism is defined as unknown, because either the mechanism has yet to be elucidated in the experimental 012 * literature, or the paper(s) curated thus far do not define the mechanism, and a full literature search has 013 * yet to be performed. 014 */ 015 ACTIVATION, 016 /** 017 * General inhibition. Compounds that inhibit the specified enzyme activity by an unknown mechanism. The 018 * mechanism is defined as unknown, because either the mechanism has yet to be elucidated in the experimental 019 * literature, or the paper(s) curated thus far do not define the mechanism, and a full literature search has 020 * yet to be performed. 021 */ 022 INHIBITION, 023 024 /** 025 * @deprecated LEVEL 1 workaround 026 */ 027 ACTIVATION_UNKMECH, 028 /** 029 * @deprecated LEVEL 1 workaround 030 */ 031 INHIBITION_UNKMECH, 032 /** 033 * Allosteric inhibitors decrease the specified enzyme activity by binding reversibly to the enzyme and 034 * inducing a conformational change that decreases the affinity of the enzyme to its substrates without 035 * affecting its VMAX. Allosteric inhibitors can be competitive or noncompetitive inhibitors, therefore, 036 * those inhibition categories can be used in conjunction with this category. 037 */ 038 INHIBITION_ALLOSTERIC, 039 /** 040 * Competitive inhibitors are compounds that competitively inhibit the specified enzyme activity by binding 041 * reversibly to the enzyme and preventing the substrate from binding. Binding of the inhibitor and substrate 042 * are mutually exclusive because it is assumed that the inhibitor and substrate can both bind only to the free 043 * enzyme. A competitive inhibitor can either bind to the active site of the enzyme, 044 * directly excluding the substrate from binding there, or it can bind to another site on the enzyme, 045 * altering the conformation of the enzyme such that the substrate can not bind to the active site. 046 */ 047 INHIBITION_COMPETITIVE, 048 /** 049 * Irreversible inhibitors are compounds that irreversibly inhibit the specified enzyme activity by binding to 050 * the enzyme and dissociating so slowly that it is considered irreversible. For example, alkylating agents, 051 * such as iodoacetamide, irreversibly inhibit the catalytic activity of some enzymes by modifying cysteine 052 * side chains. 053 */ 054 INHIBITION_IRREVERSIBLE, 055 /** 056 * Noncompetitive inhibitors are compounds that noncompetitively inhibit the specified enzyme by binding 057 * reversibly to both the free enzyme and to the enzyme-substrate complex. The inhibitor and substrate may be 058 * bound to the enzyme simultaneously and do not exclude each other. However, only the enzyme-substrate complex 059 * (not the enzyme-substrate-inhibitor complex) is catalytically active. 060 */ 061 INHIBITION_NONCOMPETITIVE, 062 /** 063 * Compounds that inhibit the specified enzyme activity by a mechanism that has been characterized, 064 * but that cannot be clearly classified as irreversible, competitive, noncompetitive, uncompetitive, 065 * or allosteric. 066 */ 067 INHIBITION_OTHER, 068 /** 069 * Uncompetitive inhibitors are compounds that uncompetitively inhibit the specified enzyme activity by binding 070 * reversibly to the enzyme-substrate complex but not to the enzyme alone. 071 */ 072 INHIBITION_UNCOMPETITIVE, 073 /** 074 * Nonallosteric activators increase the specified enzyme activity by means other than allosteric. 075 */ 076 ACTIVATION_NONALLOSTERIC, 077 /** 078 * Allosteric activators increase the specified enzyme activity by binding reversibly to the enzyme and 079 * inducing a conformational change that increases the affinity of the enzyme to its substrates without 080 * affecting its VMAX. 081 */ 082 ACTIVATION_ALLOSTERIC 083}