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Nucleotide sequence of the Schizosaccharomyces pombe lys1 + Gene and Similarities of the lys1 + protein to peptide antibiotic synthetases
Author(s) -
Bhattacherjee Vasker,
Bhattacharjee Jnanendra K.
Publication year - 1998
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/(sici)1097-0061(19980330)14:5<479::aid-yea236>3.0.co;2-t
Subject(s) - schizosaccharomyces pombe , biology , adenylylation , gene , protein subunit , nucleic acid sequence , peptide , schizosaccharomyces , biochemistry , peptide sequence , genetics , microbiology and biotechnology , saccharomyces cerevisiae , biosynthesis
The 4·2 kbp lys1 + gene of Schizosaccharomyces pombe encoding the large subunit of α‐aminoadipate reductase (EC1.2.1.31), an enzyme specific to lysine synthesis in higher fungi, was completely sequenced at the nucleotide level from pLYS1H. The S. pombe lys1 + gene product consists of 1415 amino acid residues and has a putative molecular weight of 155·8 kDa. The encoded protein converts α‐aminoadipic acid to α‐aminoadipate‐δ‐semialdehyde by an ATP‐mediated adenylation. Analysis of the sequence showed that the putative protein encoded by lys1 + shares strong homology with the peptide antibiotic synthetases which also use an adenylation step. The sequence data reported in this paper have been submitted to GenBank database (Washington DC, USA) under the Accession Number U15923. © 1998 John Wiley & Sons, Ltd.