[42] Carboxypeptidase T
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Publisher
Elsevier
Reference13 articles.
1. Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T A metalloenzyme endowed with dual substrate specificity
2. Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris
3. Proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Purification and characterization of the carboxypeptidase.
Cited by 19 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Preparation, Crystallization, and Preliminary X-Ray Diffraction Study of Mutant Carboxypeptidase T Bearing the Hydrophilized Primary Specificity Pocket;Crystallography Reports;2021-05
2. Structure of the microbial carboxypeptidase T complexed with the transition state analog N-sulfamoyl-l-lysine;Biophysical Chemistry;2021-03
3. The nature of the ligand’s side chain interacting with the S1'-subsite of metallocarboxypeptidase T (from Thermoactinomyces vulgaris) determines the geometry of the tetrahedral transition complex;PLOS ONE;2019-12-30
4. Three-Dimensional Structure of a Mutant of Carboxypeptidase T from Thermoactinomyces vulgaris Bearing an Implanted S1' Subsite of Pancreatic Carboxypeptidase B Complexed with a Product Analog;Crystallography Reports;2019-09
5. Mobile Loop in the Active Site of Metallocarboxypeptidases as an Underestimated Determinant of Substrate Specificity;Biochemistry (Moscow);2018-12
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