| EC |
2.8.1.16 |
| Accepted name: |
L-aspartate semialdehyde sulfurtransferase |
| Reaction: |
hydrogen sulfide + L-aspartate 4-semialdehyde + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = L-homocysteine + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster |
| Other name(s): |
MA1821 (locus name); MJ0100 (locus name) |
| Systematic name: |
hydrogen sulfide:L-aspartate-4-semialdehyde sulfurtransferase |
| Comments: |
The enzyme, characterized from the archaeon Methanosarcina acetivorans, participates in an L-methionine biosysnthetic pathway found in most of the methanogenic archaea. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Rauch, B.J., Gustafson, A. and Perona, J.J. Novel proteins for homocysteine biosynthesis in anaerobic microorganisms. Mol. Microbiol. 94 (2014) 1330–1342. [PMID: 25315403] |
| 2. |
Allen, K.D., Miller, D.V., Rauch, B.J., Perona, J.J. and White, R.H. Homocysteine is biosynthesized from aspartate semialdehyde and hydrogen sulfide in methanogenic archaea. Biochemistry 54 (2015) 3129–3132. [PMID: 25938369] |
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| [EC 2.8.1.16 created 2019] |
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