Substrate Specificity of Escherichia coli Peptidyl-Transferase
نویسندگان
چکیده
منابع مشابه
Substrate specificity of a glucose permease of Escherichia coli.
Rogers, Dexter (Utah State University, Logan) and Shon-hua Yu. Substrate specificity of a glucose permease of Escherichia coli. J. Bacteriol. 84:877-881. 1962.-A study was made of d-galactose uptake by galactose-negative Escherichia coli strain A (Weigle). Uptake probably occurred through a glucose-permease system, because d-glucose and a variety of nonmetabolizable glucose derivatives inhibite...
متن کاملSubstrate Specificity and Induction of Thymidine Phosphorylase in Escherichia Coli.
Purified preparations from Escherichia coli of the enzyme thymidine :orthophosphate deoxyribosyltransferase (EC 2.4. 2.4) or thymidine phosphorylase are specific for deoxyribose lphosphate. A number of pyrimidine bases function in the reaction, however, including uracil, 5-bromoand 5-aminouracil, 2-thiothymine, and 2-thiouracil, whereas deoxycytidine is inert (1). The level of enzyme in extract...
متن کاملSubstrate specificity of the pyruvate dehydrogenase complex from Escherichia coli.
The investigation of the substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli allows a description of the binding region of pyruvate. Substrate analogs with electronegative substitutions in the methyl group show a strong competitive inhibition of the overall reaction of the pyruvate dehydrogenase complex. The most efficient inhibitor is fluoropyruvate which has a mo...
متن کاملSubstrate specificity of the Escherichia coli outer membrane protease OmpP.
Escherichia coli OmpP is an F episome-encoded outer membrane protease that exhibits 71% amino acid sequence identity with OmpT. These two enzymes cleave substrate polypeptides primarily between pairs of basic amino acids. We found that, like OmpT, purified OmpP is active only in the presence of lipopolysaccharide. With optimal peptide substrates, OmpP exhibits high catalytic efficiency (k(cat)/...
متن کاملMapping of Escherichia coli ribosomal components involved in peptidyl transferase activity.
The method of affinity labeling has been used to identify protein components of 50S ribosomal subunits involved in peptidyl transferase activity. E. coli 50S ribosomal subunits were mapped by reaction with the N-bromoacetyl analog of chloramphenicol, an antibiotic known to interact specifically with the active center of the enzyme. The synthetic analog competes with chloramphenicol in binding t...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1970
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1970.tb00998.x