Purification and characterization of a new NAD(+)-dependent enzyme, L-tartrate decarboxylase, from Pseudomonas sp. group Ve-2.
A new enzyme, L-tartrate decarboxylase, was found in cells of Pseudomonas sp. group Ve-2. The enzyme was purified to homogeneity and characterized. The enzyme requires K+, Mg2+, and NAD+ for L-tartrate decarboxylation. The dependence of the enzymatic decarboxylation on NAD+ suggests that the decarboxylation involves redox reactions of the substrate. The enzyme catalyzes NAD(+)-linked oxidative decarboxylation of D-malate as well. The enzyme is composed of four subunits with identical molecular weight (Mr 40,000). The apparent Michaelis constants for L-tartrate and NAD+ are 1.1 mM, respectively. The cofactor requirements and the physical properties of the enzyme were similar to those of L-tartrate dehydrogenase-D-malate dehydrogenase from Rhodopseudomonas sphaeroides, and tartrate dehydrogenase from P. putida.
Furuyoshi
S
S
Department of Chemistry, Faculty of Engineering and Design, Kyoto Institute of Technology.
Nawa
Y
Y
Kawabata
N
N
Tanaka
H
H
Soda
K
K
D002262:Carboxy-Lyases / Q000302:isolation & purification / Q000378:metabolism*; D002413:Cations, Divalent; D002852:Chromatography, Ion Exchange; D004589:Electrophoresis, Disc; D007202:Indicators and Reagents; D007525:Isoelectric Focusing; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity
D002413:Cations, Divalent; D007202:Indicators and Reagents; D046911:Macromolecular Substances; D009243:NAD; D002262:Carboxy-Lyases; C072662:L-tartrate decarboxylase