Cloning, sequencing and overexpression of the leucine dehydrogenase gene from Bacillus cereus.
The L-leucine dehydrogenase gene from Bacillus cereus (DSM 626) was cloned from a partial genomic library and sequenced. The open reading frame has 1101 bp and codes for a protein of 39.9 kDa. The deduced amino acid sequence of the LeuDH from B. cereus shares 70-80% identity with LeuDH's from the thermophilic strains B. stearothermophilus and Thermoactinomyces intermedius. The active protein was overexpressed in Escherichia coli to yield approximately 30% of the total soluble protein.
Stoyan
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Institut für Enzymtechnologie, Heinrich-Heine Universität Düsseldorf in der KFA-Jülich, Germany.
Recktenwald
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Kula
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MR
D000594:Amino Acid Oxidoreductases / Q000737:chemistry / Q000235:genetics*; D000595:Amino Acid Sequence; D001409:Bacillus cereus / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D017931:DNA Primers; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D050803:Leucine Dehydrogenase; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016366:Open Reading Frames; D016133:Polymerase Chain Reaction; D016415:Sequence Alignment; D017421:Sequence Analysis
D017931:DNA Primers; D000594:Amino Acid Oxidoreductases; D050803:Leucine Dehydrogenase