Per ulteriori informazioni selezionare i riferimenti di interesse.
Application of linear free energy relationships to the serpin-proteinase inhibition mechanism
FEBS LETTERS
Identification of active site residues in E-coli ketopantoate reductase bymutagenesis and chemical rescue
BIOCHEMISTRY
Benzoic acid derivatives induce recovery of catalytic activity in the partially inactive Met208Lys mutant of human glutathione transferase A1-1
JOURNAL OF MOLECULAR BIOLOGY
Role of lysine 39 of alanine racemase from Bacillus stearothermophilus that binds pyridoxal 5 '-phosphate - Chemical rescue studies of Lys(39)-> Ala mutant
JOURNAL OF BIOLOGICAL CHEMISTRY
PROTON-TRANSFER IN BENZYL ALCOHOL-DEHYDROGENASE DURING CATALYSIS - ALTERNATE PROTON-RELAY ROUTES
Biochemistry
ACTIVATION OF E350A MUTANT MALTODEXTRIN PHOSPHORYLASE BY EXOGENOUSLY ADDED ACETATE
Protein engineering
CHEMICAL RESCUE OF ASP237-]ALA AND LYS358-]ALA MUTANTS IN THE LACTOSEPERMEASE OF ESCHERICHIA-COLI
Biochemistry
THE REACTION CATALYZED BY ESCHERICHIA-COLI ASPARTATE-AMINOTRANSFERASEHAS MULTIPLE PARTIALLY RATE-DETERMINING STEPS, WHILE THAT CATALYZED BY THE Y225F MUTANT IS DOMINATED BY KETIMINE HYDROLYSIS
Biochemistry
MUTAGENESIS OF ACTIVE-SITE RESIDUES IN TYPE-I DEHYDROQUINASE FROM ESCHERICHIA-COLI - STALLED CATALYSIS IN A HISTIDINE TO ALANINE MUTANT
The Journal of biological chemistry
EXAMINING THE STRUCTURAL AND CHEMICAL FLEXIBILITY OF THE ACTIVE-SITE BASE, LYS-258, OF ESCHERICHIA-COLI ASPARTATE-AMINOTRANSFERASE BY REPLACEMENT WITH UNNATURAL AMINO-ACIDS
Biochemistry
OF SITE-DIRECTED MUTAGENESIS AND ALTERNATIVE SUBSTRATES TO ASSIGN THEPROTOTROPIC GROUPS IMPORTANT TO CATALYSIS BY ESCHERICHIA-COLI ASPARTATE-AMINOTRANSFERASE
Biochemistry
EXTENT OF PROTON-TRANSFER IN THE TRANSITION-STATES OF THE REACTION CATALYZED BY THE DELTA(5)-3-KETOSTEROID ISOMERASE OF COMAMONAS (PSEUDOMONAS) TESTOSTERONI - SITE-SPECIFIC REPLACEMENT OF THE ACTIVE-SITE BASE,ASPARTATE-38, BY THE WEAKER BASE ALANINE-3-SULFINATE
Biochemistry
LYSINE-87 IN THE BETA-SUBUNIT OF TRYPTOPHAN SYNTHASE THAT FORMS AN INTERNAL ALDIMINE WITH PYRIDOXAL-PHOSPHATE SERVES CRITICAL ROLES IN TRANSIMINATION, CATALYSIS, AND PRODUCT RELEASE
The Journal of biological chemistry