B6db activities : frbh

	Activities \| Families \| Sequences \| Fold types \| References \| Help


	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
	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
Family	frbh (0)

Links	Enzyme (activities) frbh BRENDA (activities) frbh KEGG (pathways) frbh PLPMDB (PLP mutants) frbh

References	Johannes TW, DeSieno MA, Griffin BM, Thomas PM, Kelleher NL, Metcalf WW, Zhao H. (2010) Deciphering the late biosynthetic steps of antimalarial compound FR-900098. Chemistry & biology 17 57-64. Articles on frbh

last changed	2018/04/11 13:07

Family