Enzymes
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- Name help_outline 5-hydroxypentanoate Identifier CHEBI:16230 Charge -1 Formula C5H9O3 InChIKeyhelp_outline PHOJOSOUIAQEDH-UHFFFAOYSA-M SMILEShelp_outline OCCCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acetyl-CoA Identifier CHEBI:57288 (Beilstein: 8468140) help_outline Charge -4 Formula C23H34N7O17P3S InChIKeyhelp_outline ZSLZBFCDCINBPY-ZSJPKINUSA-J SMILEShelp_outline CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 352 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 5-hydroxy-pentanoyl-CoA Identifier CHEBI:57357 Charge -4 Formula C26H40N7O18P3S InChIKeyhelp_outline AMSWDUXCNHIVFP-ZMHDXICWSA-J SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)CCCCO 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acetate Identifier CHEBI:30089 (Beilstein: 1901470; CAS: 71-50-1) help_outline Charge -1 Formula C2H3O2 InChIKeyhelp_outline QTBSBXVTEAMEQO-UHFFFAOYSA-M SMILEShelp_outline CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 174 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:23496 | RHEA:23497 | RHEA:23498 | RHEA:23499 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Properties of 5-hydroxyvalerate CoA-transferase from Clostridium aminovalericum.
Eikmanns U., Buckel W.
5-Hydroxyvalerate CoA-transferase from Clostridium aminovalericum, strain T2-7, was purified approximately 100-fold to homogeneity. The molecular mass of the native enzyme was determined by three different methods to be 178 +/-11 kDa; that of the subunit was 47 kDa, indicating a homotetrameric str ... >> More
5-Hydroxyvalerate CoA-transferase from Clostridium aminovalericum, strain T2-7, was purified approximately 100-fold to homogeneity. The molecular mass of the native enzyme was determined by three different methods to be 178 +/-11 kDa; that of the subunit was 47 kDa, indicating a homotetrameric structure. The following CoA esters acted as substrates (decreasing specificity, V/Km): 5-hydroxyvaleryl-CoA greater than propionyl-CoA greater than acetyl-CoA greater than (Z)-5-hydroxy-2-pentenoyl-CoA greater than butyryl-CoA greater than valeryl-CoA. 4-Pentenoate and 3-pentenoate were also activated by acetyl-CoA to the corresponding CoA esters, whereas crotonate, (E)-5-hydroxy-2-pentenoate, (E)-2-pentenoate and 2,4-pentadienoate were not attacked. 5-Hydroxyvalerate CoA-transferase showed ping-pong kinetics and was inactivated by sodium boranate only in the presence of a CoA substrate. This indicated the formation of a thiolester between a specific carboxyl group of the enzyme and CoASH during the course of the reaction. The CoA-transferase was inhibited by ATP and CTP, slightly by ADP, GTP and UTP, but not by AMP. The inhibition by ATP was competitive towards CoA esters and noncompetitive towards acetate. << Less
Biol Chem Hoppe Seyler 371:1077-1082(1990) [PubMed] [EuropePMC]