Journal
CHEMBIOCHEM
Volume 11, Issue 2, Pages 266-271Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.200900600
Keywords
antibiotics; balhimycin; beta-hydroxytyrosine; glycopeptides; thioesterases; vancomycin
Funding
- Deutsche Forschungsgemeinschaft [DFG Pe 438/16-1, 16-2, DFG Su 239/3-3]
- EU [COMBIG-TOP-LSHB-CT-2003-503491]
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The putative hydrolase gene bhp from the balhimycin biosynthetic gene cluster has been cloned and overexpressed in Escherichia coli. The corresponding enzyme Bhp was purified to homogeneity by nickel-chelating chromatography and characterized. Although Bhp has sequence similarities to hydrolases with haloperoxidase/perhydrolase activity, it did not show any enzymatic activity with standard haloperoxidase/perhydrolase substrates (e.g., monochlorodimedone and phenol red), nonspecific esterase substrates (such as p-nitrophenyl acetate, p-nitrophenyl phosphate and S-thiophenyl acetate) or the model lactonase substrate dihydrocoumarin. However, Bhp could be shown to catalyse the hydrolysis of S-beta-hydroxytyrosyl-N-acetyl cysteamine thioester (beta-OH-Tyr-SNAC) with 15 times the efficiency Of S-L-tyrosyl-N-acetyl cysteamine thioester (L-Tyr-SNAC). This is in agreement with the suggestion that Bhp is involved in balhimycin biosynthesis, during which it was supposed to catalyse the hydrolysis of beta-OH-Tyr-S-PCP (PCP= peptidyl carrier protein) to free beta-hydroxytyrosine (beta-OH-Tyr) and strongly suggests that Bhp is a thioesterase with high substrate specificity for PCP-bound beta-OH-Tyr and not a haloperoxidase/perhydrolase or nonspecific esterase.
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