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Literature summary for 1.3.1.56 extracted from

  • Sylvestre, M.
    Genetically modified organisms to remediate polychlorinated biphenyls. Where do we stand? (2004), Int. Biodeter. Biodegrad., 54, 153-162.
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Burkholderia sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ Comamonas testosteroni
-
biphenyl-2,3-diol + NADH
-
?
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ Burkholderia sp.
-
biphenyl-2,3-diol + NADH
-
?
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ Burkholderia sp. LB400
-
biphenyl-2,3-diol + NADH
-
?
additional information Comamonas testosteroni enzyme catalyzes the second step in the biphenyl catabolic degradation pathway, substrate spectrum of the organism in vivo, overview ?
-
?
additional information Burkholderia sp. enzyme catalyzes the second step in the biphenyl catabolic degradation pathway, substrate spectrum of the organism in vivo, overview ?
-
?
additional information Burkholderia sp. LB400 enzyme catalyzes the second step in the biphenyl catabolic degradation pathway, substrate spectrum of the organism in vivo, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Burkholderia sp.
-
enzyme BphB
-
Burkholderia sp. LB400
-
enzyme BphB
-
Comamonas testosteroni
-
gene bphB
-

Purification (Commentary)

Purification (Comment) Organism
-
Comamonas testosteroni
-
Burkholderia sp.

Reaction

Reaction Comment Organism Reaction ID
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ = biphenyl-2,3-diol + NADH + H+ catalytic triad is formed by the conserved residues SEr142, Tyr153, and Lys159 Comamonas testosteroni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2',5,5'-tetrachlorobiphenyl + NAD+
-
Comamonas testosteroni 2,2',5,5'-tetrachloro-3,4-dihydroxybiphenyl + NADH
-
?
2,2',5,5'-tetrachlorobiphenyl + NAD+
-
Burkholderia sp. 2,2',5,5'-tetrachloro-3,4-dihydroxybiphenyl + NADH
-
?
2,2',5,5'-tetrachlorobiphenyl + NAD+
-
Burkholderia sp. LB400 2,2',5,5'-tetrachloro-3,4-dihydroxybiphenyl + NADH
-
?
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
Comamonas testosteroni biphenyl-2,3-diol + NADH
-
?
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
Burkholderia sp. biphenyl-2,3-diol + NADH
-
?
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
Burkholderia sp. LB400 biphenyl-2,3-diol + NADH
-
?
additional information enzyme catalyzes the second step in the biphenyl catabolic degradation pathway, substrate spectrum of the organism in vivo, overview Comamonas testosteroni ?
-
?
additional information enzyme catalyzes the second step in the biphenyl catabolic degradation pathway, substrate spectrum of the organism in vivo, overview Burkholderia sp. ?
-
?
additional information enzyme shows a broad substrate specificity Comamonas testosteroni ?
-
?
additional information enzyme shows a broad substrate specificity Burkholderia sp. ?
-
?
additional information enzyme catalyzes the second step in the biphenyl catabolic degradation pathway, substrate spectrum of the organism in vivo, overview Burkholderia sp. LB400 ?
-
?
additional information enzyme shows a broad substrate specificity Burkholderia sp. LB400 ?
-
?

Synonyms

Synonyms Comment Organism
2,3-dihydro-2,3-dehydroxybiphenyl-2,3-dehydrogenase
-
Comamonas testosteroni
2,3-dihydro-2,3-dehydroxybiphenyl-2,3-dehydrogenase
-
Burkholderia sp.
BphB
-
Comamonas testosteroni
BphB
-
Burkholderia sp.
More enzyme belongs to the short-chain alcohol dehydrogenase/reductase family Comamonas testosteroni
More enzyme belongs to the short-chain alcohol dehydrogenase/reductase family Burkholderia sp.

Cofactor

Cofactor Comment Organism Structure
additional information NADP+ is a poor cofactor, probably due to Asp at position 36 Comamonas testosteroni
NAD+
-
Burkholderia sp.
NAD+ 260fold preferred over NADP+ Comamonas testosteroni