Bacillus intermedius glutamyl endopeptidase. Molecular cloning and nucleotide sequence of the structural gene

The glutamyl endopeptidase gene of Bacillus intermedius was cloned from a genomic library expressed in Bacillus subtilis and sequenced (EMBL accession number Y15136). The encoded preproenzyme contains 303 amino acid residues; the mature 23-kDa enzyme consists of 215 residues. The mature enzyme revea...

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Bibliographic Details
Published in:Journal of Protein Chemistry 1999-01, Vol.18 (1), p.21-27
Main Authors: Rebrikov, D V, Akimkina, T V, Shevelev, A B, Demidyuk, I V, Bushueva, A M, Kostrov, S V, Chestukhina, G G, Stepanov, V M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Bacillus - enzymology
Bacillus - genetics
Bacillus intermedius
Bacillus licheniformis
Bacillus subtilis
Bacillus subtilis - genetics
Bacteriology
Base Sequence
Carboxyl group
Cloning
Cloning, Molecular
Enzymes
Gene Library
Genes, Bacterial
Genomics
Glutamyl endopeptidase
Models, Biological
Molecular biology
Molecular Sequence Data
Nucleotide sequence
Nucleotides
Phylogeny
Proteins
Recombinant Proteins
Residues
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Serine Endopeptidases - genetics
Staphylococcus aureus - genetics
Structural members
Substrates
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Summary:The glutamyl endopeptidase gene of Bacillus intermedius was cloned from a genomic library expressed in Bacillus subtilis and sequenced (EMBL accession number Y15136). The encoded preproenzyme contains 303 amino acid residues; the mature 23-kDa enzyme consists of 215 residues. The mature enzyme reveals 38% of identical residues when aligned with the glutamyl endopeptidase from Bacillus licheniformis, whereas only five invariant residues were found among all known glutamyl endopeptidases. The amino acid residues that form the catalytic triad (H47, D98, and S171) as well as H186 participating in the binding of the substrate carboxyl group were identified. It seems that the structural elements responsible for the function of glutamyl endopeptidases from various sources are highly variable.
ISSN:0277-8033
1572-3887
1573-4943
DOI:10.1023/A:1020639230985