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Literature summary for 1.14.13.223 extracted from

  • Giessen, T.W.; Kraas, F.I.; Marahiel, M.A.
    A four-enzyme pathway for 3,5-dihydroxy-4-methylanthranilic acid formation and incorporation into the antitumor antibiotic sibiromycin (2011), Biochemistry, 50, 5680-5692.
    View publication on PubMed
Search for more literature for 1.14.13.223

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Streptosporangium sibiricum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.743
-
 3-hydroxy-4-methylanthranilyl-[aryl-carrier protein] pH 7.0, 30°C Streptosporangium sibiricum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39900
-
-
 Streptosporangium sibiricum

Organism

Organism UniProt Comment Textmining
Streptosporangium sibiricum C0LTM1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-hydroxy-4-methylanthranilyl-[aryl-carrier protein] + NADH + H+ + O2
-
 Streptosporangium sibiricum 3,5-dihydroxy-4-methylanthranilyl-[aryl-carrier protein] + NAD+ + H2O SibG hydroxylates the C5 position of peptidyl-carrier protein-bound 3-hydroxy-4-methylanthranilic acid ?

Subunits

Subunits Comment Organism
? x * 39900, SDS-PAGE, recombinant His-tagged protein Streptosporangium sibiricum

Synonyms

Synonyms Comment Organism
sibG
-
 Streptosporangium sibiricum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.48
-
 3-hydroxy-4-methylanthranilyl-[aryl-carrier protein] pH 7.0, 30°C Streptosporangium sibiricum

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Streptosporangium sibiricum

General Information

General Information Comment Organism
physiological function biosynthesis of the antitumor antibiotic sibiromycin. Starting from 3-hydroxykynurenine, the SAM-dependent methyltransferase SibL converts the substrate to its 4-methyl derivative, followed by hydrolysis through the action of the PLP-dependent kynureninase SibQ, leading to 3-hydroxy-4-methylanthranilic acid formation. Subsequently the nonribosomal peptide synthetase SibE activates 3-hydroxy-4-methylanthranilic acid and tethers it to its thiolation domain, where it is hydroxylated at the C5 position by the FAD/NADH-dependent hydroxylase SibG yielding the fully substituted anthranilate moiety found in sibiromycin Streptosporangium sibiricum