Enzymes
| UniProtKB help_outline | 37,550 proteins |
| Enzyme class help_outline |
|
| GO Molecular Function help_outline |
|
Reaction participants Show >> << Hide
- Name help_outline (2R,3S)-3-isopropylmalate Identifier CHEBI:35121 Charge -2 Formula C7H10O5 InChIKeyhelp_outline RNQHMTFBUSSBJQ-CRCLSJGQSA-L SMILEShelp_outline CC(C)[C@@H]([C@@H](O)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,142 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 4-methyl-2-oxopentanoate Identifier CHEBI:17865 (Beilstein: 3904096) help_outline Charge -1 Formula C6H9O3 InChIKeyhelp_outline BKAJNAXTPSGJCU-UHFFFAOYSA-M SMILEShelp_outline CC(C)CC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 16 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (Beilstein: 1900390; CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 980 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADH Identifier CHEBI:57945 (Beilstein: 3869564) help_outline Charge -2 Formula C21H27N7O14P2 InChIKeyhelp_outline BOPGDPNILDQYTO-NNYOXOHSSA-L SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,073 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:32271 | RHEA:32272 | RHEA:32273 | RHEA:32274 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| Gene Ontology help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline | ||||
| EcoCyc help_outline |
Publications
-
THE ABSOLUTE CONFIGURATION OF ALPHA-HYDROXY-BETA-CARBOXYISOCAPROIC ACID (3-ISOPROPYLMALIC ACID), AN INTERMEDIATE IN LEUCINE BIOSYNTHESIS.
CALVO J.M., STEVENS C.M., KALYANPUR M.G., UMBARGER H.E.
Biochemistry 3:2024-2027(1964) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.
-
Purification and properties of beta-isopropylmalate dehydrogenase.
Parsons S.J., Burns R.O.
J. Biol. Chem. 244:996-1003(1969) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
-
Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase.
Nemeth A., Svingor A., Pocsik M., Dobo J., Magyar C., Szilagyi A., Gal P., Zavodszky P.
The comparison of the three-dimensional structures of thermophilic (Thermus thermophilus) and mesophilic (Escherichia coli) 3-isopropylmalate dehydrogenases (IPMDH, EC 1.1.1.85) suggested that the existence of extra ion pairs in the thermophilic enzyme found in the intersubunit region may be an im ... >> More
The comparison of the three-dimensional structures of thermophilic (Thermus thermophilus) and mesophilic (Escherichia coli) 3-isopropylmalate dehydrogenases (IPMDH, EC 1.1.1.85) suggested that the existence of extra ion pairs in the thermophilic enzyme found in the intersubunit region may be an important factor for thermostability. As a test of our assumption, glutamine 200 in the E. coli enzyme was turned into glutamate (Q200E mutant) to mimic the thermophilic enzyme at this site by creating an intersubunit ion pair which can join existing ion clusters. At the same site in the thermophilic enzyme we changed glutamate 190 into glutamine (E190Q), hereby removing the corresponding ion pair. These single amino acid replacements resulted in increased thermostability of the mesophilic and decreased thermostability of the thermophilic enzyme, as measured by spectropolarimetry and differential scanning microcalorimetry. << Less
FEBS Lett 468:48-52(2000) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
-
The biosynthesis of leucine. III. The conversion of alpha-hydroxy-beta-carboxyisocaproate to alpha-ketoisocaproate.
Burns R.O., Umbarger H.E., Gross S.R.
Biochemistry 2:1053-1058(1963) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
Multi-step reaction: RHEA:10892 and RHEA:25078