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Biochemistry|March 1, 1994
Probing the role of histidine-372 in zinc binding and the catalytic mechanism of Escherichia coli alkaline phosphatase by site-specific mutagenesisX Xu, X Q Qin, E R KantrowitzBiochemistry|March 21, 1989
Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylaseJ W Stebbins, W Xu, E R KantrowitzJournal of Molecular Biology|July 29, 1998
A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase results in an extreme T-state structureM K Williams, B Stec, E R KantrowitzProceedings of the National Academy of Sciences of the United States of America|July 1, 1990
Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesiumH M Ke, Y P Zhang, W N LipscombProceedings of the National Academy of Sciences of the United States of America|June 1, 1978
Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residueS M Landfear, D R Evans, W N LipscombProceedings of the National Academy of Sciences of the United States of America|August 15, 1991
Leucine aminopeptidase: bestatin inhibition and a model for enzyme-catalyzed peptide hydrolysisS K Burley, P R David, W N LipscombProceedings of the National Academy of Sciences of the United States of America|July 1, 1984
Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolutionH M Ke, R B Honzatko, W N LipscombProceedings of the National Academy of Sciences of the United States of America|November 1, 1978
Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphateH L Monaco, J L Crawford, W N LipscombJournal of Molecular Biology|February 5, 1987
2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartateK L Krause, K W Volz, W N LipscombBiochemistry|April 4, 1995
Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallographyV Villeret, S Huang, Y Zhang, et al.Pageof 22