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Nucleotide sequence of the maltotetraohydrolase gene from Pseudomonas saccharophila
Author(s) -
Zhou Jianhua,
Baba Tadashi,
Takano Toshiya,
Kobayashi Shoichi,
Arai Yuji
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81056-7
Subject(s) - gene , amylase , nucleic acid sequence , biochemistry , coding region , signal peptide , pseudomonas , peptide sequence , enzyme , nucleotide , biology , protein primary structure , thermophile , chemistry , genetics , bacteria
The nucleotide sequence of the Pseudomonas saccharophila gene encoding maltotetraohydrolase (G 4 ‐forming amylase) has been determined. The coding region for the G 4 ‐forming amylase precursor contained 1653 nucleotides. The deduced precursor protein included an N‐terminal 21‐residue putative signal peptide; the deduced mature form of G 4 ‐forming amylase contains 530 amino acid residues with a calculated molecular mass of 57 740 Da. Sequence similarities between the G 4 ‐forming amylase and other amylolytic enzymes of species ranging from prokaryotes to eukaryotes are quite limited. However, three regions, which are involved in both the catalytic and substrate‐binding sites of various amylolytic enzymes, are highly conserved in the G 4 ‐forming amylase of P. saccharophila .