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The α‐amylase from the yellow meal worm: complete primary structure, crystallization and preliminary X‐ray analysis
Author(s) -
Strobl Stefan,
Gomis-Rüth Franz-Xaver,
Maskos Klaus,
Frank Gerhard,
Huber Robert,
Glockshuber Rudi
Publication year - 1997
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/s0014-5793(97)00451-1
Subject(s) - edman degradation , amylase , complementary dna , protein primary structure , orthorhombic crystal system , biochemistry , enzyme , biology , peptide sequence , homology (biology) , residue (chemistry) , homology modeling , crystallization , chemistry , amino acid , microbiology and biotechnology , gene , crystallography , crystal structure , organic chemistry
The α‐amylase from Tenebrio molitor larvae (TMA) was purified from a crude larval extract. After removal of the N‐terminal pyroglutamate residue and identification of the following 17 residues by Edman sequencing, the cDNA of mature TMA was cloned from larval mRNA. The encoded enzyme consists of 471 amino acid residues and has 57–79% sequence identity to other insect α‐amylases and also shows high homology to the mammalian enzymes. TMA was crystallized in form of well‐ordered orthorhombic crystals of space group P2 1 2 1 2 1 diffracting beyond 1.6 Å resolution with unit cell dimensions of a=51.24 Å, b=93.46 Å, c=96.95 Å. TMA may serve as model system for the future analysis of interactions between insect α‐amylase and proteinaceous plant inhibitors on the molecular level.