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Literature summary for 1.14.13.23 extracted from

  • Westphal, A.H.; Tischler, D.; van Berkel, W.J.H.
    Natural diversity of FAD-dependent 4-hydroxybenzoate hydroxylases (2021), Arch. Biochem. Biophys., 702, 108820 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene mobA, phylogenetic analysis Comamonas testosteroni

Protein Variants

Protein Variants Comment Organism
V257A a directed evolution study reveals that 3HB4H from Comamonas testosteroni strain GZ39 is considerably active with 4-hydroxybenzoate and that this activity increases in the V257A variant. The same variant slowly converts phenol to catechol, an activity not observed with the wild-type enzyme Comamonas testosteroni

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-hydroxybenzoate + NADPH + H+ + O2 Comamonas testosteroni
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3,4-dihydroxybenzoate + NADP+ + H2O
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?

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni Q6SSJ6
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-hydroxybenzoate + NADPH + H+ + O2
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Comamonas testosteroni 3,4-dihydroxybenzoate + NADP+ + H2O
-
?
additional information enzyme 3HB4H catalyzes an ortho-hydroxylation reaction Comamonas testosteroni ?
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-

Synonyms

Synonyms Comment Organism
3-hydroxybenzoate 4-hydroxylase
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Comamonas testosteroni
3HB4H
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Comamonas testosteroni
FAD-dependent 4-hydroxybenzoate hydroxylase
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Comamonas testosteroni
MobA
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Comamonas testosteroni

Cofactor

Cofactor Comment Organism Structure
FAD
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Comamonas testosteroni
NADPH
-
Comamonas testosteroni

General Information

General Information Comment Organism
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 Comamonas testosteroni
additional information FAD-dependent hydroxybenzoate hydroxylase enzymes structure comparisons, overview Comamonas testosteroni