Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Streptosporangium sibiricum |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
39900 | - |
- |
Streptosporangium sibiricum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptosporangium sibiricum | C0LTM1 | - |
- |
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 | Comment | Organism |
---|---|---|
? | x * 39900, SDS-PAGE, recombinant His-tagged protein | Streptosporangium sibiricum |
Synonyms | Comment | Organism |
---|---|---|
sibG | - |
Streptosporangium sibiricum |
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 | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Streptosporangium sibiricum |
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 |