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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.1.9 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.9 0.0187
-
NADH pH 7.5, 25°C Xanthomonas oryzae
1.3.1.9 0.293
-
crotonyl-CoA pH 7.5, 25°C Xanthomonas oryzae

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.9 Xanthomonas oryzae Q2P9J6
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.3.1.9 FabV
-
Xanthomonas oryzae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.1.9 22.25
-
crotonyl-CoA pH 7.5, 25°C Xanthomonas oryzae

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.9 NADH
-
Xanthomonas oryzae

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.3.1.9 75
-
crotonyl-CoA pH 7.5, 25°C Xanthomonas oryzae