Affiliation:
1. Marine Biotechnology Institute, Kamaishi Laboratories, 3-75-1 Heita, Kamaishi, Iwate 026, Japan
Abstract
ABSTRACT
trans
-2′-Carboxybenzalpyruvate hydratase-aldolase was purified from a phenanthrene-degrading bacterium,
Nocardioides
sp. strain KP7, and characterized. The purified enzyme was found to have molecular masses of 38 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 113 kDa by gel filtration chromatography. Thus, the homotrimer of the 38-kDa subunit constituted an active enzyme. The
K
m
and
k
cat values of this enzyme for
trans
-2′-carboxybenzalpyruvate were 50 μM and 13 s
−1
, respectively.
trans
-2′-Carboxybenzalpyruvate was transformed to 2-carboxybenzaldehyde and pyruvate by the action of this enzyme. The structural gene for this enzyme was cloned and sequenced; the length of this gene was 996 bp. The deduced amino acid sequence of this enzyme exhibited homology to those of
trans
-2′-hydroxybenzalpyruvate hydratase-aldolases from
Pseudomonas putida
PpG7 and
Pseudomonas
sp. strain C18.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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