| EC |
6.3.4.24 |
| Accepted name: |
tyramine—L-glutamate ligase |
| Reaction: |
ATP + tyramine + L-glutamate = ADP + phosphate + γ-glutamyltyramine |
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For diagram of methanofuran biosynthesis, click here |
| Other name(s): |
mfnD (gene name) |
| Systematic name: |
tyramine:L-glutamate γ-ligase (ADP-forming) |
| Comments: |
The enzyme, which has been characterized from the archaea Methanocaldococcus fervens, participates in the biosynthesis of the cofactor methanofuran. Requires a divalent cation for activity, with Mn2+ giving the highest activity, followed by Mg2+, Co2+, Zn2+, and Fe2+. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Wang, Y., Xu, H., Harich, K.C. and White, R.H. Identification and characterization of a tyramine-glutamate ligase (MfnD) Involved in methanofuran biosynthesis. Biochemistry 53 (2014) 6220–6230. [DOI] [PMID: 25211225] |
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| [EC 6.3.4.24 created 2014] |
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