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frbh |
Description |
CMP-5'-2-amino-phosphonobutyrate decarboxylase (4.1.1.-) |
Catalyzed reaction |
CMP-5'-2-ammino-phophonobutyrate =
CMP-5'-3-amminopropylphosphonate + CO(2) |
Cofactor |
Pyridoxal phosphate |
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The enzyme frbh has two distinct domains, an N-terminal nucleotide transferase domain followed by a PLP-dependent
aminotransferase/decarboxylase domain. The nucleotide transferase domain catalyzes the convertion of 4-phosphono-2-aminobutyrate to
CMP-5'-2-amino-phosphonobutyrate.
The enzyme from Streptomyces rubellomurinus is involved in the biosynthetic pathway of the antimalarial antibiotic FR-900098. |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) frbh
BRENDA (activities) frbh
KEGG (pathways) frbh
PLPMDB (PLP mutants) frbh
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References |
Articles on frbh |
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last changed |
2018/04/11 13:07 |
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