PqqC/D, which converts a biosynthetic intermediate to pyrroloquinoline quinone.
PqqC/D was purified from Escherichia coli transformant. The purified enzyme converted an intermediate that accumulated in a pqqC mutant of Methylobacterium extorquens AM1 to PQQ. The reaction did not show any dependence of NAD(P)H that was observed in the crude extract before purification. PqqC/D reacted with the intermediate stoichiometrically, but not catalytically. When partially purified proteins from the crude extract of E. coli were added to the reaction mixture, the rate of PQQ production increased dependent on the amount of NADPH added and the total amount of PQQ produced increased.
Toyama
Hirohide
H
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, 753-8515, Yamaguchi, Japan. toyama@agr.yamaguchi-u.ac.jp
Fukumoto
Hiroyuki
H
Saeki
Megumi
M
Matsushita
Kazunobu
K
Adachi
Osao
O
Lidstrom
Mary E
ME
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D020601:Methylobacterium extorquens / Q000201:enzymology*; D009249:NADP / Q000494:pharmacology; D045542:PQQ Cofactor; D017434:Protein Structure, Tertiary; D015363:Quinolones / Q000378:metabolism*; D011809:Quinones / Q000378:metabolism*; D017384:Sequence Deletion
D001426:Bacterial Proteins; C095467:PqqC protein, Bacteria; C091163:PqqD protein, Methylobacterium extorquens; D015363:Quinolones; D011809:Quinones; D009249:NADP; D045542:PQQ Cofactor