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Biochemistry|December 25, 1979
Conformations and electronic structures of oxidized and reduced isoalloxazineD A Dixon, D L Lindner, B Branchaud, et al.
The Journal of Biological Chemistry|October 15, 1989
Site-specific mutation of Tyr240----Phe in the catalytic chain of Escherichia coli aspartate transcarbamylase. Consequences for kinetic mechanismY Hsuanyu, F C Wedler, E R Kantrowitz, et al.
The Journal of Biological Chemistry|January 8, 2000
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 transcarbamoylaseJ B Sakash, R S Chan, H Tsuruta, et al.
Biochemistry|November 1, 1988
Function of arginine-166 in the active site of Escherichia coli alkaline phosphataseA Chaidaroglou, D J Brezinski, S A Middleton, et al.
Protein Science : a Publication of the Protein Society|July 1, 1999
The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativityC Macol, M Dutta, B Stec, et al.
The Journal of Biological Chemistry|May 16, 2001
Domain bridging interactions. A necessary contribution to the function and structure of Escherichia coli aspartate transcarbamoylaseJ B Sakash, M K Williams, H Tsuruta, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 1, 1980
Isolation and preliminary characterization of single amino acid substitution mutants of aspartate carbamoyltransferaseE R Kantrowitz, J Foote, H W Reed, et al.
Biochimica Et Biophysica Acta|March 16, 1989
Kinetic consequences of site-specific mutation of Glu-239----Gln in E. coli aspartate transcarbamylase: comparison with catalytic subunits and Phe-240 mutant enzymeY Hsuanyu, F C Wedler, S A Middleton, et al.
Biochemistry|October 17, 1995
Fructose-1,6-bisphosphatase: arginine-22 is involved in stabilization of the T allosteric stateG Lu, M K Williams, E L Giroux, et al.
The Journal of Biological Chemistry|October 7, 1994
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 interfaceD P Baker, J W Stebbins, E DeSena, et al.
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