The alpha-amylase from the yellow meal worm: complete primary structure, crystallization and preliminary X-ray analysis.
FEBS Lett
; 409(1): 109-14, 1997 Jun 02.
Article
em En
| MEDLINE
| ID: mdl-9199514
ABSTRACT
The alpha-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 alpha-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 A resolution with unit cell dimensions of a = 51.24 A, b = 93.46 A, c = 96.95 A. TMA may serve as model system for the future analysis of interactions between insect alpha-amylase and proteinaceous plant inhibitors on the molecular level.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Tenebrio
/
Alfa-Amilases
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1997
Tipo de documento:
Article
País de afiliação:
Suíça