Literature summary for 1.3.1.9 extracted from

Li, H.; Zhang, X.; Bi, L.; He, J.; Jiang, T.
Determination of the crystal structure and active residues of FabV, the enoyl-ACP reductase from Xanthomonas oryzae (2011), PLoS ONE, 6, e26743.

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.6 A resolution, space group P212121. The model consists of one monomer in the asymmetric unit which is composed of 13 alpha-helices and 11 beta-strands, representing a canonical Rossmann fold architecture. In addition to the conserved residues Y236 and K245 in the Y-X8-K motif, Y53, D111 and Y226 are key residues implicated in the reductase activity, and F113 and T276 are also important for enzyme function	Xanthomonas oryzae

Crystallization (Comment)

Organism

to 1.6 A resolution, space group P212121. The model consists of one monomer in the asymmetric unit which is composed of 13 alpha-helices and 11 beta-strands, representing a canonical Rossmann fold architecture. In addition to the conserved residues Y236 and K245 in the Y-X8-K motif, Y53, D111 and Y226 are key residues implicated in the reductase activity, and F113 and T276 are also important for enzyme function

Xanthomonas oryzae

Protein Variants

Protein Variants	Comment	Organism
D111A	inactive	Xanthomonas oryzae
F113A	restores fatty acid synthesis in an Escherichia coli fabI mutant strain to wild-type level	Xanthomonas oryzae
K245A	inactive	Xanthomonas oryzae
K245R	inactive	Xanthomonas oryzae
S50A	restores fatty acid synthesis in an Escherichia coli fabI mutant strain to wild-type level	Xanthomonas oryzae
T276A	restores fatty acid synthesis in an Escherichia coli fabI mutant strain to wild-type level	Xanthomonas oryzae
V246A	restores fatty acid synthesis in an Escherichia coli fabI mutant strain to wild-type level	Xanthomonas oryzae
Y226F	restores fatty acid synthesis in an Escherichia coli fabI mutant strain to wild-type level	Xanthomonas oryzae
Y236A	inactive	Xanthomonas oryzae
Y236F	inactive	Xanthomonas oryzae
Y53A	partly restores fatty acid synthesis in an Escherichia coli fabI mutant strain	Xanthomonas oryzae
Y53F	restores fatty acid synthesis in an Escherichia coli fabI mutant strain to wild-type level	Xanthomonas oryzae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0187	-	NADH	pH 7.5, 25°C	Xanthomonas oryzae
0.293	-	crotonyl-CoA	pH 7.5, 25°C	Xanthomonas oryzae

Organism

Organism	UniProt	Comment	Textmining
Xanthomonas oryzae	Q2P9J6	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
crotonyl-CoA + NADH + H+	-	Xanthomonas oryzae	butyryl-CoA + NAD+	-	?

Synonyms

Synonyms	Comment	Organism
FabV	-	Xanthomonas oryzae

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
22.25	-	crotonyl-CoA	pH 7.5, 25°C	Xanthomonas oryzae

Cofactor

Cofactor	Comment	Organism	Structure
NADH	-	Xanthomonas oryzae

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
75	-	crotonyl-CoA	pH 7.5, 25°C	Xanthomonas oryzae