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Title: Conserved enzymes mediate the early reactions of carotenoid biosynthesis in nonphotosynthetic and photosynthetic prokaryotes

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (United States)
;  [1];  [2]
  1. Univ. of California, Berkeley (United States) Lawrence Berkeley Lab., CA (United States)
  2. Lawrence Berkeley Lab., CA (United States)

Carotenoids comprise one of the most widespread classes of pigments found in nature. The first reactions of C{sub 40} carotenoid biosynthesis proceed through common intermediates in all organisms, suggesting the evolutionary conservation of early enzymes from this pathway. The authors report here the nucleotide sequence of three genes from the carotenoid biosynthesis gene cluster of Erwinia herbicola, a nonphotosynthetic epiphytic bacterium, which encode homologs of the CrtB, CrtE, and CrtI proteins of Rhodobacter capsulatus, a purple nonsulfur photosynthetic bacterium. CrtB (prephytoene pyrophosphate synthase), CrtE (phytoene synthase), and CrtI (phytoene dehydrogenase) are required for the first three reactions specific to the carotenoid branch of general isoprenoid metabolism. All three dehydrogenases possess a hydrophobic N-terminal domain containing a putative ADP-binding {beta}{alpha}{beta} fold characteristic of enzymes known to bind FAD or NAD(P) cofactors. These data indicate the structural conservation of early carotenoid biosynthesis enzymes in evolutionary diverse organisms.

DOE Contract Number:
AC03-76SF00098
OSTI ID:
6145198
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 87:24; ISSN 0027-8424
Country of Publication:
United States
Language:
English