Identification and characterization of a bacterial glutamic peptidase.
Identification and characterization of a bacterial glutamic peptidase.
复制标题
DOI：
10.1186/1471-2091-11-47
复制
发表时间：
2010-12-01
期刊：
影响因子：
--
通讯作者：
Lassen SF
中科院分区：
文献类型：
--
作者：
Jensen K;Østergaard PR;Wilting R;Lassen SF
来自Merops家族G1的谷氨酰胺petidass是一组独特的宠物酶，其特征是由谷氨酸和谷氨酰胺保留，最佳活性，对酸性pH值的最佳活性以及对微生物衍生的蛋白酶抑制剂的最佳活性源自丝状真菌的特征。
我们报告了源自热酸性细菌的细菌谷氨酸肽（PEPG1）的首次表征谷氨酸/谷氨酰胺催化二元组和许多高度保守的基序强烈支持将PEPG1作为谷氨酰胺肽酶将PEPG1和其他推定的细菌和古细菌酶放置在与真菌谷氨酸彼得非洲蛋白酶分开的聚类中，表明细菌和真菌谷氨酸pepi酶的分歧和独立的进化，在pepg1上纯化，在pepg1上纯化。离子交换色谱法。温度和pH值为60°C和pH 3-4，与对家族G1的真菌成员观察到的值一致。肽酶。
基于获得的结果，我们建议可以将PEPG1添加到Merops家族G1中，作为第一个特征性细菌成员。
Glutamic peptidases, from the MEROPS family G1, are a distinct group of peptidases characterized by a catalytic dyad consisting of a glutamate and a glutamine residue, optimal activity at acidic pH and insensitivity towards the microbial derived protease inhibitor, pepstatin. Previously, only glutamic peptidases derived from filamentous fungi have been characterized. We report the first characterization of a bacterial glutamic peptidase (pepG1), derived from the thermoacidophilic bacteria Alicyclobacillus sp. DSM 15716. The amino acid sequence identity between pepG1 and known fungal glutamic peptidases is only 24-30% but homology modeling, the presence of the glutamate/glutamine catalytic dyad and a number of highly conserved motifs strongly support the inclusion of pepG1 as a glutamic peptidase. Phylogenetic analysis places pepG1 and other putative bacterial and archaeal glutamic peptidases in a cluster separate from the fungal glutamic peptidases, indicating a divergent and independent evolution of bacterial and fungal glutamic peptidases. Purification of pepG1, heterologously expressed in Bacillus subtilis, was performed using hydrophobic interaction chromatography and ion exchange chromatography. The purified peptidase was characterized with respect to its physical properties. Temperature and pH optimums were found to be 60°C and pH 3-4, in agreement with the values observed for the fungal members of family G1. In addition, pepG1 was found to be pepstatin-insensitive, a characteristic signature of glutamic peptidases. Based on the obtained results, we suggest that pepG1 can be added to the MEROPS family G1 as the first characterized bacterial member.
登录
查看更多内容
影响因子：
2.9
作者：
Bhattacharya, Aneerban;Wunderlich, Zeba;Montelione, Gaetano T.
通讯作者：
Montelione, Gaetano T.
DOI：
10.1080/00021369.1974.10861522
发表时间：
1974-01-01
期刊：
AGRICULTURAL AND BIOLOGICAL CHEMISTRY
影响因子：
--
作者：
ODA, K;MURAO, S
通讯作者：
MURAO, S
影响因子：
14.9
作者：
Dereeper A;Guignon V;Blanc G;Audic S;Buffet S;Chevenet F;Dufayard JF;Guindon S;Lefort V;Lescot M;Claverie JM;Gascuel O
通讯作者：
Gascuel O
影响因子：
14.9
作者：
Bru C;Courcelle E;Carrère S;Beausse Y;Dalmar S;Kahn D
通讯作者：
Kahn D
影响因子：
5.8
作者：
Arnold, K;Bordoli, L;Schwede, T
通讯作者：
Schwede, T