| 1-aminocyclopropane-1-carboxylate deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.99.7 | ||||||||
| CAS no. | 69553-48-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a 1-aminocyclopropane-1-carboxylate deaminase ( EC 3.5.99.7) is an enzyme that catalyzes the chemical reaction
- 1-aminocyclopropane-1-carboxylate + H2O 2-oxobutanoate + NH3
Thus, the two substrates of this enzyme are 1-aminocyclopropane-1-carboxylate and H2O, whereas its two products are 2-oxobutanoate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing). This enzyme is also called 1-aminocyclopropane-1-carboxylate endolyase (deaminating). This enzyme participates in propanoate metabolism. It employs one cofactor, pyridoxal phosphate.
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1RQX, 1TYZ, 1TZ2, 1TZJ, 1TZK, and 1TZM.
- Honma M, Shimomura T (1978). "Metabolism of 1-aminocyclopropane-1-carboxylic acid". Agric. Biol. Chem. 42 (10): 1825–1831. doi: 10.1271/bbb1961.42.1825.
- Wakatsuki S, Yokoi D, Murakami T, Honma M, Tanaka I (2000). "Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus". J. Biol. Chem. 275 (44): 34557–34565. doi: 10.1074/jbc.M004681200. PMID 10938279.
| 1-aminocyclopropane-1-carboxylate deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.99.7 | ||||||||
| CAS no. | 69553-48-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a 1-aminocyclopropane-1-carboxylate deaminase ( EC 3.5.99.7) is an enzyme that catalyzes the chemical reaction
- 1-aminocyclopropane-1-carboxylate + H2O 2-oxobutanoate + NH3
Thus, the two substrates of this enzyme are 1-aminocyclopropane-1-carboxylate and H2O, whereas its two products are 2-oxobutanoate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing). This enzyme is also called 1-aminocyclopropane-1-carboxylate endolyase (deaminating). This enzyme participates in propanoate metabolism. It employs one cofactor, pyridoxal phosphate.
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1RQX, 1TYZ, 1TZ2, 1TZJ, 1TZK, and 1TZM.
- Honma M, Shimomura T (1978). "Metabolism of 1-aminocyclopropane-1-carboxylic acid". Agric. Biol. Chem. 42 (10): 1825–1831. doi: 10.1271/bbb1961.42.1825.
- Wakatsuki S, Yokoi D, Murakami T, Honma M, Tanaka I (2000). "Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus". J. Biol. Chem. 275 (44): 34557–34565. doi: 10.1074/jbc.M004681200. PMID 10938279.