Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.13.44 extracted from

  • Lazar, J.T.; Shuvalova, L.; Rosas-Lemus, M.; Kiryukhina, O.; Satchell, K.J.F.; Minasov, G.
    Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida with PobA from other Pseudomonas spp. and other monooxygenases (2019), Acta Crystallogr. Sect. F, 75, 507-514 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.44

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-hydroxybiphenyl + NADH + H+ + O2 Pseudomonas nitroreducens
-
 2,3-dihydroxybiphenyl + NAD+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas nitroreducens O06647
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hydroxybiphenyl + NADH + H+ + O2
-
 Pseudomonas nitroreducens 2,3-dihydroxybiphenyl + NAD+ + H2O
-
 ?
additional information comparisons of substrate binding structures, overview Pseudomonas nitroreducens ?
-
-

Synonyms

Synonyms Comment Organism
2-hydroxybiphenyl 3-monooxygenase
-
 Pseudomonas nitroreducens
HbpA
-
 Pseudomonas nitroreducens

Cofactor

Cofactor Comment Organism Structure
FAD binding domain structure comparisons, overview Pseudomonas nitroreducens
NADH
-
 Pseudomonas nitroreducens

General Information

General Information Comment Organism
additional information sequence comparisons, three-dimensional enzyme structure analysis, and structure comparisons with 2-hydroxybiphenyl 3-monooxygenase (HbpA, PDB ID 4cy8) from Pseudomonas nitroreducens and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) from Mesorhizobium japonicum, overview. Despite having only 14% similarity in their primary sequences, pairwise structure alignments of PobA from Pseudomonas putida with HbpA from Pseudomonas nitroreducens and MHPCO from Mesorhizobium japonicum reveal local similarities between these structures. Key residues in the FAD-binding and substrate-binding sites of PobA are highly conserved spatially across the proteins from all three species. Key secondary-structure elements important for catalysis, such as the betaalphabeta fold, beta-sheet wall and alpha12 helix, are conserved across this expanded class of oxygenases Pseudomonas nitroreducens
physiological function HbpA hydroxylates its substrate 2-hydroxybiphenyl to 2,3-dihydroxybiphenyl Pseudomonas nitroreducens