OSTENDORP, R and LIEBL, W and SCHURIG, H and JAENICKE, R (1993) THE L-LACTATE DEHYDROGENASE GENE OF THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA-MARITIMA CLONED BY COMPLEMENTATION IN ESCHERICHIA-COLI. EUROPEAN JOURNAL OF BIOCHEMISTRY, 216 (3). pp. 709-715. ISSN 0014-2956,
Full text not available from this repository.Abstract
The gene for a L(+)-lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima was cloned by complementation of an Escherichia coli pfl. ldh mutant. The gene is part of a 4.5 kb SauIIIA fragment obtained by partial digestion of the Thermotoga genome. The DNA fragment was physically mapped and the putative Shine-Dalgarno sequence within the non-coding region determined. The gene contains 960 bp, including the stop codon, corresponding to 319 amino acids/subunit of the homotetrameric enzyme. Part of the amino acid sequence was confirmed by Edman degradation of peptides obtained from nanomolar quantities of the purified enzyme by tryptic digestion. A comparison of the amino acid sequence with those of known prokaryotiC L-lactate dehydrogenases reveals a high similarity, especially with the enzyme from thermophilic sources, where up to 48% identity is found. The gene was expressed as an active enzyme in a heterologous host.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | AMINO-ACID-SEQUENCE; SP-NOV REPRESENTS; NUCLEOTIDE-SEQUENCE; BACILLUS-STEAROTHERMOPHILUS; MESOPHILIC BACTERIA; D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; PROTEIN STABILITY; CLONING; EXPRESSION; ENZYME; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:42 |
| URI: | https://pred.uni-regensburg.de/id/eprint/53768 |
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