Electron acquisition system constructed from an NAD-independent D-lactate dehydrogenase and cytochrome c2 in Rhodopseudomonas palustris No. 7.

Content Provider	Semantic Scholar
Author	Horikiri, Shunsuke Aizawa, Yoshiyuki Kai, Taiki Amachi, Seigo Shinoyama, Hirofumi Fujii, Takaaki
Copyright Year	2004
Abstract	The activities of NAD-independent D- and L-lactate dehydrogenases (D-LDH, L-LDH) were detected in Rhodopseudomonas palustris No. 7 grown photoanaerobically on lactate. One of these enzymes, D-LDH, was purified as an electrophoretically homogeneous protein (M(r), about 235,000; subunit M(r) about 57,000). The pI was 5.0. The optimum pH and temperature of the enzyme were pH 8.5 and 50 degrees C, respectively. The Km of the enzyme for D-lactate was 0.8 mM. The enzyme had narrow substrate specificity (D-lactate and DL-2-hydroxybutyrate). The enzymatic activity was competitively inhibited by oxalate (Ki, 0.12 mM). The enzyme contained a FAD cofactor. Cytochrome c(2) was purified from strain No. 7 as an electrophoretically homogeneous protein. Its pI was 9.4. Cytochrome c(2) was reduced by incubating with D-LDH and D-lactate.
Starting Page	299
Ending Page	304
Page Count	6
File Format	PDF HTM / HTML
Alternate Webpage(s)	https://www.jstage.jst.go.jp/article/bbb/68/3/68_3_516/_pdf/-char/en
PubMed reference number	15056881v1
Volume Number	68
Issue Number	3
Journal	Bioscience, biotechnology, and biochemistry
Language	English
Access Restriction	Open
Subject Keyword	Contain (action) Cytochromes c2 Flavin-Adenine Dinucleotide L-Lactate dehydrogenase (cytochrome) Lactate Dehydrogenase Lactic acid Nicotinamide adenine dinucleotide (NAD) Oxalates Oxidoreductase Potassium Iodide Rhodopseudomonas Substrate Specificity incubated
Content Type	Text
Resource Type	Article