Published in Biochemistry on September 05, 1989
Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase. Microbiol Mol Biol Rev (2001) 1.02
A molecular mechanism for pyrimidine and purine nucleotide control of aspartate transcarbamoylase. Proc Natl Acad Sci U S A (1992) 0.90
Asymmetric allosteric signaling in aspartate transcarbamoylase. ACS Chem Biol (2010) 0.86
Metal ion involvement in the allosteric mechanism of Escherichia coli aspartate transcarbamoylase. Biochemistry (2012) 0.76
The use of nucleotide analogs to evaluate the mechanism of the heterotropic response of Escherichia coli aspartate transcarbamoylase. Protein Sci (2000) 0.76
Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway. J Biol Chem (1985) 1.65
An improved colorimetric assay for aspartate and ornithine transcarbamylases. Anal Biochem (1981) 1.58
A revised mechanism for the alkaline phosphatase reaction involving three metal ions. J Mol Biol (2000) 1.37
Escherichia coli aspartate carbamoyltransferase: the probing of crystal structure analysis via site-specific mutagenesis. Protein Eng (1991) 1.23
A model of the transition state in the alkaline phosphatase reaction. J Biol Chem (1999) 1.22
An essential residue at the active site of aspartate transcarbamylase. J Biol Chem (1976) 1.12
Function of arginine-166 in the active site of Escherichia coli alkaline phosphatase. Biochemistry (1988) 1.09
Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase. Biochemistry (1989) 1.08
Interaction of tetraiodofluorescein with aspartate transcarbamylase and its isolated catalytic and regulatory subunits. J Biol Chem (1975) 1.07
A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase. Proc Natl Acad Sci U S A (1999) 1.06
Glutamic acid residue 98 is critical for catalysis in pig kidney fructose-1,6-bisphosphatase. Biochem Biophys Res Commun (1996) 1.00
A possible model for the concerted allosteric transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies. Biochemistry (1988) 1.00
Conversion of a magnesium binding site into a zinc binding site by a single amino acid substitution in Escherichia coli alkaline phosphatase. J Biol Chem (1993) 1.00
Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutions. J Mol Biol (1983) 0.98
Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase. Nat Struct Biol (2001) 0.97
Zn(II)-induced cooperativity of Escherichia coli ornithine transcarbamoylase. Proc Natl Acad Sci U S A (1982) 0.96
Identification of a trans-acting regulatory factor involved in the control of the pyrimidine pathway in E. coli. Mol Gen Genet (1983) 0.96
Magnesium in the active site of Escherichia coli alkaline phosphatase is important for both structural stabilization and catalysis. Biochemistry (1993) 0.95
Trapping and visualization of a covalent enzyme-phosphate intermediate. Nat Struct Biol (1997) 0.95
The conserved residues glutamate-37, aspartate-100, and arginine-269 are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase. Biochemistry (1993) 0.95
Relationship between domain closure and binding, catalysis, and regulation in Escherichia coli aspartate transcarbamylase. Biochemistry (1988) 0.94
Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases. J Mol Biol (1995) 0.93
Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase. Biochemistry (1990) 0.92
The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sites. J Biol Chem (1991) 0.92
Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102. J Mol Biol (1998) 0.92
The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site-specific mutagenesis. FEBS Lett (1999) 0.92
Involvement of tryptophan 209 in the allosteric interactions of Escherichia coli aspartate transcarbamylase using single amino acid substitution mutants. J Mol Biol (1986) 0.91
Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylase. J Mol Biol (1990) 0.90
Mutation of Arg-166 of alkaline phosphatase alters the thio effect but not the transition state for phosphoryl transfer. Implications for the interpretation of thio effects in reactions of phosphatases. Biochemistry (2000) 0.89
The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chain. Proc Natl Acad Sci U S A (1990) 0.88
A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase results in an extreme T-state structure. J Mol Biol (1998) 0.88
A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylase. Biochemistry (1989) 0.88
A cis-proline to alanine mutant of E. coli aspartate transcarbamoylase: kinetic studies and three-dimensional crystal structures. Biochemistry (2000) 0.87
Functionally important arginine residues of aspartate transcarbamylase. J Biol Chem (1977) 0.87
Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylase. Biochemistry (1990) 0.87
Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylase. Biochemistry (1988) 0.87
Characterization of the aspartate transcarbamoylase from Methanococcus jannaschii. J Biol Chem (2000) 0.87
Rate-determining step of Escherichia coli alkaline phosphatase altered by the removal of a positive charge at the active center. Biochemistry (1999) 0.87
The contribution of individual interchain interactions to the stabilization of the T and R states of Escherichia coli aspartate transcarbamoylase. J Biol Chem (2000) 0.86
Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase. J Mol Biol (1996) 0.85
Conversion of the noncooperative Bacillus subtilis aspartate transcarbamoylase into a cooperative enzyme by a single amino acid substitution. Biochemistry (1992) 0.85
Comparison of the essential arginine residue in Escherichia coli ornithine and aspartate transcarbamylases. Biochim Biophys Acta (1981) 0.85
An essential arginine residue in porcine phospholipiase A2. J Biol Chem (1980) 0.84
Catalytic-regulatory subunit interactions and allosteric effects in aspartate transcarbamylase. J Biol Chem (1987) 0.84
Why are mammalian alkaline phosphatases much more active than bacterial alkaline phosphatases? Mol Microbiol (1994) 0.84
Propagation of allosteric changes through the catalytic-regulatory interface of Escherichia coli aspartate transcarbamylase. Biochemistry (1988) 0.83
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. Protein Sci (1992) 0.83
Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase. J Biol Chem (2000) 0.83
Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase. Proc Natl Acad Sci U S A (1992) 0.83
The interaction of tetraiodofluorescein with aspartate transcarbamylase. Biochem Biophys Res Commun (1973) 0.83
Reaction of Woodward's Reagent K with pancreatic porcine phospholipase A2: modification of an essential carboxylase residue. Biochem Biophys Res Commun (1981) 0.82
Probing the regulatory site of Escherichia coli aspartate transcarbamoylase by site-specific mutagenesis. Biochemistry (1992) 0.82
Importance of the loop at residues 230-245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferase. Proc Natl Acad Sci U S A (1986) 0.82
Binding of magnesium in a mutant Escherichia coli alkaline phosphatase changes the rate-determining step in the reaction mechanism. Biochemistry (1993) 0.82
Mutations at histidine 412 alter zinc binding and eliminate transferase activity in Escherichia coli alkaline phosphatase. J Biol Chem (1994) 0.81
Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes. Protein Sci (2000) 0.81
Use of silicate sol-gels to trap the R and T quaternary conformational states of pig kidney fructose-1,6-bisphosphatase. Biochim Biophys Acta (2001) 0.81
Function of threonine-55 in the carbamoyl phosphate binding site of Escherichia coli aspartate transcarbamoylase. Biochemistry (1989) 0.81
The use of alanine scanning mutagenesis to determine the role of the N-terminus of the regulatory chain in the heterotropic mechanism of Escherichia coli aspartate transcarbamoylase. Protein Eng (1994) 0.81
Function of serine-52 and serine-80 in the catalytic mechanism of Escherichia coli aspartate transcarbamoylase. Biochemistry (1991) 0.81
Kinetics and crystal structure of a mutant Escherichia coli alkaline phosphatase (Asp-369-->Asn): a mechanism involving one zinc per active site. Protein Sci (1994) 0.81
A water-mediated salt link in the catalytic site of Escherichia coli alkaline phosphatase may influence activity. Biochemistry (1991) 0.81
Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity. Protein Sci (1996) 0.81
Fructose-1,6-bisphosphatase: arginine-22 is involved in stabilization of the T allosteric state. Biochemistry (1995) 0.80
Characterization of heterodimeric alkaline phosphatases from Escherichia coli: an investigation of intragenic complementation. J Mol Biol (2000) 0.80
The N-terminus of the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for both nucleotide binding and heterotropic effects. Biochemistry (1998) 0.80
Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure. Protein Sci (1994) 0.80
Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase. Biochemistry (1992) 0.80
Alteration of aspartate 101 in the active site of Escherichia coli alkaline phosphatase enhances the catalytic activity. Protein Eng (1989) 0.80
Room temperature phosphorescence study of phosphate binding in Escherichia coli alkaline phosphatase. Eur J Biochem (1997) 0.80
The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity. Protein Sci (1999) 0.80
Escherichia coli alkaline phosphatase: X-ray structural studies of a mutant enzyme (His-412-->Asn) at one of the catalytically important zinc binding sites. Protein Sci (1995) 0.79
Engineered complementation in Escherichia coli aspartate transcarbamoylase. Heterotropic regulation by quaternary structure stabilization. J Biol Chem (1996) 0.79
Probing the role of histidine-372 in zinc binding and the catalytic mechanism of Escherichia coli alkaline phosphatase by site-specific mutagenesis. Biochemistry (1994) 0.79
Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism. J Biol Chem (1995) 0.79
Isolation and preliminary characterization of single amino acid substitution mutants of aspartate carbamoyltransferase. Proc Natl Acad Sci U S A (1980) 0.79
Direct observation of an altered quaternary-structure transition in a mutant aspartate transcarbamoylase. Proteins (1998) 0.79
Site-directed mutagenesis of a residue located in the regulatory site of Escherichia coli aspartate transcarbamoylase. Involvement of lysine 94 in effector binding and the allosteric mechanism. J Biol Chem (1988) 0.78
Amino acid substitutions at the subunit interface of dimeric Escherichia coli alkaline phosphatase cause reduced structural stability. Protein Sci (1999) 0.78
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. Protein Sci (1996) 0.78
The importance of aspartate 327 for catalysis and zinc binding in Escherichia coli alkaline phosphatase. J Biol Chem (1992) 0.78
The importance of the link between Glu204 of the catalytic chain and Arg130 of the regulatory chain for the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase. J Biol Chem (1989) 0.78
Shared active sites of fructose-1,6-bisphosphatase. Arginine 243 mediates substrate binding and fructose 2,6-bisphosphate inhibition. J Biol Chem (1994) 0.78
Analysis of mutant Escherichia coli aspartate transcarbamylases isolated from a series of suppressed pyrB nonsense strains. J Mol Biol (1981) 0.77
The influence of the regulatory chain amino acids Glu-62 and IIe-12 on the heterotropic properties of Escherichia coli aspartate transcarbamoylase. Biochemistry (1998) 0.77
Structure of a single amino acid mutant of aspartate carbamoyltransferase at 2.5-A resolution: implications for the cooperative mechanism. Biochemistry (1989) 0.77
Overexpression and purification of the trimeric aspartate transcarbamoylase from Bacillus subtilis. Protein Expr Purif (1995) 0.77
Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sites. Biochemistry (1996) 0.76
The use of nucleotide analogs to evaluate the mechanism of the heterotropic response of Escherichia coli aspartate transcarbamoylase. Protein Sci (2000) 0.76
Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylase. Protein Sci (1995) 0.76
Structural consequences of a one atom mutation on aspartate transcarbamylase from E. coli. FEBS Lett (1989) 0.76
AMP inhibition of pig kidney fructose-1,6-bisphosphatase. Biochim Biophys Acta (2001) 0.76
Glutamic acid 86 is important for positioning the 80's loop and arginine 54 at the active site of Escherichia coli aspartate transcarbamoylase and for the structural stabilization of the C1-C2 interface. J Biol Chem (1994) 0.76
The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure. Protein Sci (1996) 0.76
Interaction of tetraiodofluorescein with a modified form of aspartate transcarbamylase. Proc Natl Acad Sci U S A (1977) 0.75
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 transcarbamoylase. Protein Sci (2002) 0.75
Domain bridging interactions. A necessary contribution to the function and structure of Escherichia coli aspartate transcarbamoylase. J Biol Chem (2001) 0.75