GilR, an unusual lactone-forming enzyme involved in gilvocarcin biosynthesis.
Last at last: The terminal step of the gilvocarcin V (GV) biosynthetic pathway is an unusual lactone formation. Here we show that the enzyme, GilR, dehydrogenates the hemiacetal moiety of pregilvocarcin V to the lactone found in GV by using covalently bound FAD.
Kharel
Madan Kumar
MK
University of Kentucky, Department of Pharmaceutical Sciences, College of Pharmacy, 725 Rose Street, Lexington, KY 40536-0082, USA.
Pahari
Pallab
P
Lian
Hui
H
Rohr
Jürgen
J
D000970:Antineoplastic Agents / Q000737:chemistry*; D055162:Biocatalysis; D003374:Coumarins / Q000737:chemistry; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry; D006027:Glycosides / Q000096:biosynthesis* / Q000737:chemistry; D007700:Kinetics; D007783:Lactones / Q000737:chemistry*; D005810:Multigene Family; D010088:Oxidoreductases / Q000378:metabolism*
D000970:Antineoplastic Agents; D003374:Coumarins; D006027:Glycosides; D007783:Lactones; D005182:Flavin-Adenine Dinucleotide; C031781:gilvocarcin V; D010088:Oxidoreductases