Abstract
The mannopeptimycins (MPPs) are potent glycopeptide antibiotics that contain both D and L forms of the unique, arginine-derived amino acid β-hydroxyenduracididine (βhEnd). The product of the mppO gene in the MPP biosynthetic cluster resembles several non-heme iron, α-ketoglutarate- dependent oxygenases, such as VioC and clavaminate synthase. The role of MppO in βhEnd biosynthesis was confirmed through inactivation of mppO, which yielded a strain that produced dideoxy-MPPs, indicating that mppO is essential for generating the β-hydroxy functionality for both βhEnd residues. Characterization in vitro of recombinant His6-MppO expressed in E. coli revealed that MppO selectively hydroxylates the β carbon of free L-enduracididine.
Original language | English (US) |
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Pages (from-to) | 1163-1168 |
Number of pages | 6 |
Journal | Chemistry and Biology |
Volume | 12 |
Issue number | 11 |
DOIs | |
State | Published - Nov 2005 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Pharmacology
- Drug Discovery
- Clinical Biochemistry