EC number:2.3.1.37
Enzyme
Download| EC Tree |
| 2. Transferases |
| 2.3 Acyltransferases |
| 2.3.1 Transferring groups other than aminoacyl groups |
| ID: | 2.3.1.37 | ||
|---|---|---|---|
| Description: | 5-aminolevulinate synthase. | ||
| Alternative Name: |
Delta-aminolevulinate synthase. Delta-ALA synthetase. ALAS. 5-aminolevulinic acid synthase. | ||
| Prosite: | PDOC00518; | ||
| PDB: |
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| Cath: | 1.10.1200.70; 3.30.460.30; 4.10.92.10; 3.40.50.720; 3.40.640.10; 3.90.1150.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.3.1.37 |
| BRENDA Enzyme Link: | BRENDA 2.3.1.37 |
| KEGG Enzyme Link: | KEGG2.3.1.37 |
| BioCyc Enzyme Link: | BioCyc 2.3.1.37 |
| ExPASy Enzyme Link: | ExPASy2.3.1.37 |
| EC2PDB Enzyme Link: | EC2PDB 2.3.1.37 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.3.1.37 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.3.1.37 |
| IntEnz Enzyme Link: | IntEnz 2.3.1.37 |
| MEDLINE Enzyme Link: | MEDLINE 2.3.1.37 |
| RHEA:12921 | glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[S;H0;+0:4]-[*:5].[*:6]=[C;H0;+0:7](-[OH;+0:8])-[CH2;+0:9]-[*:10].[H+;H0:11]>>[*:1]-[C;H0;+0:2](=[*:3])-[CH2;+0:9]-[*:10].[*:5]-[SH;+0:4].[*:6]=[C;H0;+0:7]=[O;H0;+0:8] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| 5-Aminolevulinate synthase and the first step of heme biosynthesis. | Ferreira GC, Gong J | 1995 Apr | 7592562 |
| Soluble -aminolevulinic acid synthetase of rat liver. II. Studies related to the mechanism of enzyme action and hemin inhibition. | Scholnick PL, Hammaker LE, Marver HS | 1972 Jul 10 | 5035685 |
| Studies on delta-aminolevulinic acid synthase of Rhodopseudomonas spheroides. Reversibility of the reaction, kinetic, spectral, and other studies related to the mechanism of action. | Nandi DL | 1978 Dec 25 | 309883 |
| Human delta-aminolevulinate synthase: assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome. | Bishop DF, Henderson AS, Astrin KH | 1990 Jun | 2347585 |
| The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis. | Cox TC, Sadlon TJ, Schwarz QP, Matthews CS, Wise PD, Cox LL, Bottomley SS, May BK | 2004 Feb | 14643893 |
| Lysine-313 of 5-aminolevulinate synthase acts as a general base during formation of the quinonoid reaction intermediates. | Hunter GA, Ferreira GC | 1999 Mar 23 | 10090759 |