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

BRENDA support

Refine search

Search General Information

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 3 of 3
download as CSV
download all results as CSV
EC Number General Information Commentary Reference
Display the reaction diagram Show all sequences 6.2.1.74metabolism the loading module (LM) of Rif synthetase activates 3-amino-5-hydroxybenzoate (AHB) as AHB-AMP and links it to the phosphopantetheine arm of its thiolation domain (T1). AHB is then transferred across the non-ribosomal peptide synthase interface to the active-site cysteine of the ketosynthase domain of PKS module 1 (M1), and this second intermediate reacts with a methylmalonyl moiety to form an aryl ketide covalently bound to the M1 thiolation domain (T2). Occupancy of the T2 domain of LM-M1 by a methylmalonyl moiety triggers intermodular transfer of benzoate from the T1 domain to the KS domain, and this transthiolation event is fast relative to the initial loading of benzoate onto the T1 domain 761346
Display the reaction diagram Show all sequences 6.2.1.74physiological function during biosynthesis of mitomycin C, MitE catalyzes the reaction between aminohydroxybenzoate-AMP and MmcB to provide an aminohydroxybenzoate-ACP conjugate 762090
Display the reaction diagram Show all sequences 6.2.1.74physiological function rifamycin synthetase is primed with a 3-amino-5-hydroxybenzoate starter unit by a loading module that contains domains homologous to the adenylation and thiolation domains of nonribosomal peptide synthetases. The thiolation domain requires covalent attachment of the 4'-phosphopantetheine moiety of CoA to a conserved serine to be active. The catalytic models for the mechanism of the adenylation and thiolation didomain involve activation of 3-amino-5-hydroxybenzoate as the aryl-adenylate by the adenylation domain, followed by eventual formation of a covalent aryl thioester enzyme intermediate from attack of either aryl-CoA or the aryl-adenylate by the thiol nucleophile of the phosphopantetheine cofactor of the thiolation domain 760561
Results 1 - 3 of 3
download as CSV
download all results as CSV