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1.14.13.23: 3-hydroxybenzoate 4-monooxygenase

This is an abbreviated version!
For detailed information about 3-hydroxybenzoate 4-monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.23

Reaction

3-hydroxybenzoate
+
NADPH
+
H+
+
O2
=
3,4-dihydroxybenzoate
+
NADP+
+
H2O

Synonyms

3-hydroxybenzoate 4-hydroxylase, 3-hydroxybenzoate hydroxylase, 3-hydroxybenzoate-4-hydroxylase, 3HB4H, EC 1.14.99.13, FAD-dependent 4-hydroxybenzoate hydroxylase, m-hydroxybenzoate hydroxylase, MHBH, MobA, oxygenase, 3-hydroxybenzoate 4-mono-

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.23 3-hydroxybenzoate 4-monooxygenase

General Information

General Information on EC 1.14.13.23 - 3-hydroxybenzoate 4-monooxygenase

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
phylogenetic analysis of FAD-dependent 4-hydroxybenzoate hydroxylases and 3-hydroxybenzoate 4-hydroxylase, phylogenetic analysis and tree, overview. Enzyme structure analysis and comparisons (PDB ID pdb: 2dkh). Enzyme 3HB4H is missing a flexible loop, which is involved in flavin movement and closing-off the active site. In 3HB4H, the conserved tyrosine 222 makes a hydrogen bond with the hydroxyl group of the phenolic substrate, substrate binding pocket and structure-function analysis, homology modeling, overview. Residues Asp75 and Tyr271 might enhance the electron donating capacity of the hydroxyl group of 3-hydroxybenzoate (3-HB). The carboxyl group of 3-HB preferentially interacts with the side chains of His135 and Lys247. This ionic interaction is proposed to determine the orientation of bound substrate
metabolism
additional information
FAD-dependent hydroxybenzoate hydroxylase enzymes structure comparisons, overview