Open AccessIdentification of Lactaldehyde Dehydrogenase in Methanocaldococcus jannaschii and Its Involvement in Production of Lactate for F 420 Biosynthesis
Author(s) -
Laura L. Grochowski,
Huimin Xu,
Robert H. White
Publication year - 2006
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.188.8.2836-2844.2006
Subject(s) - biology , biosynthesis , biochemistry , nad+ kinase , aldolase a , cofactor , dehydrogenase , lactate dehydrogenase , methanococcus , archaea , gene , enzyme
One of the early steps in the biosynthesis of coenzyme F420 inMethanocaldococcus jannaschii requires generation of 2-phospho-l -lactate, which is formed by the phosphorylation ofl -lactate. Preliminary studies had shown thatl -lactate inM. jannaschii is not derived from pyruvate, and thus an alternate pathway(s) for its formation was examined. Here we report thatl -lactate is formed by the NAD+ -dependent oxidation ofl -lactaldehyde by the MJ1411 gene product. The lactaldehyde, in turn, was found to be generated either by the NAD(P)H reduction of methylglyoxal or by the aldol cleavage of fuculose-1-phosphate by fuculose-1-phosphate aldolase, the MJ1418 gene product.