Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Leisha S. Mullins"'
Publikováno v:
Biochemistry. 38:1394-1401
A linked-function analysis of the allosteric responsiveness of carbamoyl phosphate synthetase (CPS) from E. coli was performed by following the ATP synthesis reaction at low carbamoyl phosphate concentration. All three allosteric ligands, ornithine,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ae75c4f78cc9e74764ca16e84db7201
https://doi.org/10.1021/bi982097w
https://doi.org/10.1021/bi982097w
Publikováno v:
Bioorganic Chemistry. 26:255-268
The reaction catalyzed by carbamoyl phosphate synthetase (CPS) from Escherichia coli was examined for the formation of several transient intermediates. The chemical mechanism for CPS has been previously postulated to involve the formation of carboxy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2ad1b865ab6a10c3cd2b6fed1d60fb76
https://doi.org/10.1006/bioo.1998.1103
https://doi.org/10.1006/bioo.1998.1103
Publikováno v:
Biochemistry. 37:10272-10278
Carbamoyl phosphate synthetase (CPS) catalyzes the formation of carbamoyl phosphate from bicarbonate, glutamine, and two molecules of MgATP. The X-ray crystal structure of the enzyme has revealed that the two nucleotide binding sites are separated by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::599de3d9a09db63e6730789883da0cb4
https://doi.org/10.1021/bi980753m
https://doi.org/10.1021/bi980753m
Publikováno v:
Biochemistry. 36:9022-9028
1-Bromovinyl (I), Z-2-bromovinyl (II), 1,2-dibromoethyl (III), and a series of 4-(halomethyl)-2-nitrophenyl (IVa-c) diethyl phosphate esters were examined as substrates and mechanism-based inhibitors for the bacterial phosphotriesterase. All of these
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1a2fa618ccf860dd27d5a60d5bb5107
https://doi.org/10.1021/bi970680r
https://doi.org/10.1021/bi970680r
Publikováno v:
Protein Science. 5:204-211
Ribonuclease T1 (RNase T1) is a small, globular protein of 104 amino acids for which extensive thermodynamic and structural information is known. To assess the specific influence of variations in amino acid sequence on the mechanism for protein foldi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::49c0779d0cc61fb771ef5d9ebba77c04
https://doi.org/10.1002/pro.5560050203
https://doi.org/10.1002/pro.5560050203
Autor:
Marilyn F. Harmon, Farah Javid-Majd, Michelle A. Stapleton, Frank M. Raushel, Jennifer L. Grahmann, Brent A. Hanks, Leisha S. Mullins
Publikováno v:
Biochemistry. 35:14352-14361
Carbamoyl phosphate synthetase (CPS) catalyzes the formation of carbamoyl phosphate from glutamine, bicarbonate, and 2 mol of MgATP. The heterodimeric protein is composed of a small amidotransferase subunit and a larger synthetase subunit. The synthe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2aec98b1390988c2bef0dd363367a9d9
https://doi.org/10.1021/bi961183y
https://doi.org/10.1021/bi961183y
Publikováno v:
Biochemistry. 35:11918-11924
When catalyzing the formation of MgATP and carbamate from MgADP and carbamoyl phosphate, Escherichia coli carbamoyl phosphate synthetase (CPS) binds MgADP with a large negative change in heat capacity. The magnitude of this heat capacity change is no
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::676cd9a0a4823e8beace054a1137e8dd
https://doi.org/10.1021/bi961305m
https://doi.org/10.1021/bi961305m
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 5:3067-3072
The effect of Mn 2+ Mn 2+ , Mn 2+ Zn 2+ and Mn 2+ Cd 2+ reconstituted phosphotriesterase on the 31P spin lattice ( 1 T 1 ) relaxation rate of diethyl p-methoxyphenyl phosphate has been investigated. In the presence of Mn 2+ Mn 2+ phosphotriesterase,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ba992dd20007fe124888ce6e2d28846d
https://doi.org/10.1016/0960-894x(95)00539-7
https://doi.org/10.1016/0960-894x(95)00539-7
Publikováno v:
Journal of the American Chemical Society. 116:5529-5533
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8635fd10d56fea804ee0ece47394a3ea
https://doi.org/10.1021/ja00092a001
https://doi.org/10.1021/ja00092a001
Publikováno v:
Biochemistry. 32:6152-6156
The rate of hydrogen bond formation at individual amino acid residues in ribonuclease T1 (RNase T1) has been investigated by the hydrogen-deuterium exchange-2D NMR (HDEx-2D NMR) technique (Udgaonkar & Baldwin, 1988; Rder et al., 1988) to gain insight
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf7db119055f63eca3dc95710f10851c
https://doi.org/10.1021/bi00075a006
https://doi.org/10.1021/bi00075a006