In molecular biology, the condensation ___domain is a protein ___domain found in many multi-___domain enzymes which synthesise peptide antibiotics. This ___domain catalyses a condensation reaction to form peptide bonds in non-ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding ___domain (pp-binding). It has been shown that mutations in the HHXXXDG sequence motif in this ___domain abolish activity suggesting this is part of the active site.[1]
| Condensation | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of vibh, an nrps condensation enzyme | |||||||||
| Identifiers | |||||||||
| Symbol | Condensation | ||||||||
| Pfam | PF00668 | ||||||||
| Pfam clan | CL0149 | ||||||||
| InterPro | IPR001242 | ||||||||
| SCOP2 | 1l5a / SCOPe / SUPFAM | ||||||||
| |||||||||
References
edit- ^ Stachelhaus T, Mootz HD, Bergendahl V, Marahiel MA (August 1998). "Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation ___domain". J. Biol. Chem. 273 (35): 22773–81. doi:10.1074/jbc.273.35.22773. PMID 9712910.