M. Huang et al., MOLECULAR CHARACTERIZATION OF THE PSEUDOMONAS-PUTIDA 2,3-BUTANEDIOL CATABOLIC PATHWAY, FEMS microbiology letters, 124(2), 1994, pp. 141-150
The 2,3-butanediol dehydrogenase and the acetoin-cleaving system were
simultaneously induced in Pseudomonas putida PpG2 during growth on 2,3
-butanediol and on acetoin. Hybridization with a DNA probe covering th
e genes for the E1 subunits of the Alcaligenes eutrophus acetoin cleav
ing system and nucleotide sequence analysis identified acoA (975 bp),
acoB (1020 bp), acoC (1110 bp), acoX (1053 bp) and adh (1086 bp) in a
6.3-kb genomic region. The amino acid sequences deduced from acoA, aco
B, and acoC for E1 alpha (M(r) 34639), E1 beta (M(r) 37268), and E2 (M
(r) 39613) of the P. putida acetoin cleaving system exhibited striking
similarities to those of the corresponding components of the A. eutro
phus acetoin cleaving system and of the acetoin dehydrogenase enzyme s
ystem of Pelobacter carbinolicus and other bacteria. Strong sequence s
imilarities of the adh translational product (2,3-butanediol dehydroge
nase, M(r) 38361) were obtained to various alcohol dehydrogenases belo
nging to the zinc- and NAD(P)-dependent long-chain (group I) alcohol d
ehydrogenases. Expression of the P. putida ADH in Escherichia coli was
demonstrated. The aco genes and adh constitute presumably one single
operon which encodes all enzymes required for the conversion of 2,3-bu
tanediol to central metabolites.