Bibliotecas PUC-SP - Busca Integrada

Importance of the loop at residues 230-245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferase.

Por Middleton, S A, Kantrowitz, E R
Publicado em 1986

Kinetics and crystal structure of a mutant Escherichia coli alkaline phosphatase (Asp-369-->Asn): a mechanism involving one zinc per active site.

Por Tibbitts, T. T., Xu, X., Kantrowitz, E. R.
Publicado em 1994

Escherichia coli alkaline phosphatase: X-ray structural studies of a mutant enzyme (His-412-->Asn) at one of the catalytically important zinc binding sites.

Por Ma, L., Tibbitts, T. T., Kantrowitz, E. R.
Publicado em 1995

The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop...

Por Newton, C J, Kantrowitz, E R
Publicado em 1990

Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase.

Por Williams, M K, Kantrowitz, E R
Publicado em 1992

The use of nucleotide analogs to evaluate the mechanism of the heterotropic response of Escherichia coli aspartate transcarbamoylase.

Por Sakash, J. B., Tsen, A., Kantrowitz, E. R.
Publicado em 2000

Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure.

Por Tauc, P., Keiser, R. T., Kantrowitz, E. R., Vachette, P.
Publicado em 1994

Crystal structures of the active site mutant (Arg-243-->Ala) in the T and R allosteric states of pig kidney fructose-1,6-bisphosphatase expressed in Escherichia coli.

Por Stec, B., Abraham, R., Giroux, E., Kantrowitz, E. R.
Publicado em 1996

Amino acid substitutions at the subunit interface of dimeric Escherichia coli alkaline phosphatase cause reduced structural stability.

Por Martin, D. C., Pastra-Landis, S. C., Kantrowitz, E. R.
Publicado em 1999

Zn(II)-induced cooperativity of Escherichia coli ornithine transcarbamoylase.

Por Kuo, L C, Lipscomb, W N, Kantrowitz, E R
Publicado em 1982

The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure.

Por Baker, D. P., Fetler, L., Vachette, P., Kantrowitz, E. R.
Publicado em 1996

Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity.

Por Lu, G., Stec, B., Giroux, E. L., Kantrowitz, E. R.
Publicado em 1996

A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase

Por Sträter, Norbert, Sun, Lee, Kantrowitz, E. R., Lipscomb, William N.
Publicado em 1999

The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity.

Por Macol, C., Dutta, M., Stec, B., Tsuruta, H., Kantrowitz, E. R.
Publicado em 1999

Interaction of tetraiodofluorescein with a modified form of aspartate transcarbamylase.

Por Kantrowitz, E R, Jacobsberg, L B, Landfear, S M, Lipscomb, W N
Publicado em 1977

Isolation and preliminary characterization of single amino acid substitution mutants of aspartate carbamoyltransferase.

Por Kantrowitz, E R, Foote, J, Reed, H W, Vensel, L A
Publicado em 1980

Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylase.

Por Baker, D. P., Fetler, L., Keiser, R. T., Vachette, P., Kantrowitz, E. R.
Publicado em 1995

Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes.

Por Holtz, K. M., Stec, B., Myers, J. K., Antonelli, S. M., Widlanski, T. S., Kantrowitz, E. R.
Publicado em 2000

Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylas...

Por Fetler, L., Tauc, P., Baker, D.P., Macol, C.P., Kantrowitz, E.R., Vachette, P.
Publicado em 2002

Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study.

Por Stebbins, J. W., Robertson, D. E., Roberts, M. F., Stevens, R. C., Lipscomb, W. N., Kantrowitz, E. R.
Publicado em 1992