PROSITE documentation PDOC00643Alpha-isopropylmalate and homocitrate synthases signatures
Description
The following enzymes have been shown [1] to be functionally as well as evolutionary related:
- α-isopropylmalate synthase (EC 2.3.3.13) which catalyzes the first step in the biosynthesis of leucine, the condensation of acetyl-CoA and α- ketoisovalerate to form 2-isopropylmalate synthase.
- Homocitrate synthase (EC 2.3.3.14) (gene nifV) which is involved in the biosynthesis of the iron-molybdenum cofactor of nitrogenase and catalyzes the condensation of acetyl-CoA and α-ketoglutarate into homocitrate.
- Soybean late nodulin 56.
- Methanococcus jannaschii hypothetical proteins MJ0503, MJ1195 and MJ1392.
We have selected two conserved regions as signature patterns for these enzymes. The first region is located in the N-terminal section while the second region is located in the central section and contains two conserved histidine residues which could be implicated in the catalytic mechanism.
Last update:April 2006 / Pattern revised.
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Reference
| 1 | Authors | Wang S.-Z. Dean D.R. Chen J.S. Johnson J.L. |
| Title | The N-terminal and C-terminal portions of NifV are encoded by two different genes in Clostridium pasteurianum. | |
| Source | J. Bacteriol. 173:3041-3046(1991). | |
| PubMed ID | 2022611 |
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