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Literature summary for 1.14.13.172 extracted from

  • Sun, X.; Lin, Y.; Yuan, Q.; Yan, Y.
    Precursor-directed biosynthesis of 5-hydroxytryptophan using metabolically engineered E. coli (2015), ACS Synth. Biol., 4, 554-558 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
enzyme S5H is encoded in the salABCD gene cluster, which locates on the chromosome rather than on a mobile plasmid, functional recombinant expression in Escherichia coli Cupriavidus necator

Protein Variants

Protein Variants Comment Organism
additional information precursor-directed biosynthesis of 5-hydroxytryptophan using metabolically engineered Escherichia coli and involving the salicylate 5-hydroxylase from Ralstonia eutropha strain H16 Cupriavidus necator

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
salicylate + NADH + H+ + O2 Cupriavidus necator
-
2,5-dihydroxybenzoate + NAD+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Cupriavidus necator Q0KB56
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
anthranilate + NADH + H+ + O2
-
Cupriavidus necator 5-hydroxyanthranilate + NAD+ + H2O
-
?
additional information 2-aminobenzoate might be a substrate for the enzyme Cupriavidus necator ?
-
?
salicylate + NADH + H+ + O2
-
Cupriavidus necator 2,5-dihydroxybenzoate + NAD+ + H2O
-
?

Synonyms

Synonyms Comment Organism
nagG
-
Cupriavidus necator
nagG oxygenase component Cupriavidus necator
S5H
-
Cupriavidus necator
SalABCD
-
Cupriavidus necator
SALD enzyme complex component Cupriavidus necator

Cofactor

Cofactor Comment Organism Structure
additional information SalABCD requires NAD(P)H as the cofactor instead of BH4 Cupriavidus necator
NADH
-
Cupriavidus necator

General Information

General Information Comment Organism
physiological function enzyme S5H hydroxylates salicylate into gentisate and is involved in the degradation of aromatic compounds. SalD is an essential component of the S5H complex Cupriavidus necator