Structure and Function of L-Lactate Dehydrogenases from Thermophilic, Mesophilic and Psychrophilic Bacteria, IX. Identification, Isolation and Nucleotide Sequence of Two L-Lactate. Dehydrogenase Genes of the Psychrophilic BacteriumBacillus psychrosaccharolyticus
- 1 January 1990
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 371 (1) , 103-110
- https://doi.org/10.1515/bchm3.1990.371.1.103
Abstract
Two genes encoding for L-lactate dehydrogenase (LDH) from the psychrophilic bacterium Bacillus psychrosaccharolyticus (DSM6) were cloned and their nucleotide sequence determined using a pEMBL vector and gene hybridization probes. The Deduced amino-acid sequence of the gene from clone pLDH(X), which is located on a 5.87-kb HindIII-fragment, shows an identity of 86% as compared with the sequence of the wildtype LDH(P) from B. psychrosaccharolyticus and consists of 319 amino acids. Clone pLDH (P) contained a gene on a 4-kb HindIII-EcoRI fragment, of which the amino-acid sequence is identicial with the enzyme isolated from B. psychrosaccharolytic. The nucleotide sequences of LDH(P) and LDH(X) show 77% identity. Both genes are expressed in E. coli and the proteins could be isolated as shown by enzyme activity tests and determination of the N-terminal amino-acid sequence. However no expression of LDH(X) could be detected in B. psychrosaccharolyticus itself under the conditions chosen for oxygen induction of LDH. The function of the additional, non-expressed enzyme is not known.This publication has 21 references indexed in Scilit:
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