Rebrikov D V, Akimkina T V, Shevelev A B, Demidyuk I V, Bushueva A M, Kostrov S V, Chestukhina G G, Stepanov V M
Molecular Biology Department, Biological Faculty, Moscow State University, Russia.
J Protein Chem. 1999 Jan;18(1):21-7. doi: 10.1023/a:1020639230985.
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.
从在枯草芽孢杆菌中表达的基因组文库中克隆了中间芽孢杆菌的谷氨酰内肽酶基因并进行了测序（EMBL登录号Y15136）。编码的前原酶含有303个氨基酸残基；成熟的23 kDa酶由215个残基组成。当与地衣芽孢杆菌的谷氨酰内肽酶比对时，成熟酶显示出38%的相同残基，而在所有已知的谷氨酰内肽酶中仅发现五个不变残基。鉴定出形成催化三联体的氨基酸残基（H47、D98和S171）以及参与底物羧基结合的H186。似乎来自各种来源的谷氨酰内肽酶功能的结构元件高度可变。
