Page last updated: 2024-08-17

histidine and n(omega)-hydroxyarginine

histidine has been researched along with n(omega)-hydroxyarginine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Ash, DE; Dismukes, GC; Khangulov, SV; Sossong, TM	1
Ash, DE; Boucher, JL; Cama, E; Christianson, DW; Colleluori, DM; Cox, JD; Mansuy, D; Pethe, S	1

Other Studies

2 other study(ies) available for histidine and n(omega)-hydroxyarginine

Article	Year
L-arginine binding to liver arginase requires proton transfer to gateway residue His141 and coordination of the guanidinium group to the dimanganese(II,II) center. Biochemistry, 1998, Jun-09, Volume: 37, Issue:23 Topics: Animals; Arginase; Arginine; Asparagine; Binding Sites; Borates; Citrulline; Electron Spin Resonance Spectroscopy; Guanidine; Histidine; Hydrogen-Ion Concentration; Isoleucine; Liver; Lysine; Manganese; Mutagenesis, Site-Directed; Ornithine; Protons; Rats; Substrate Specificity	1998
Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase. Biochemistry, 2001, Mar-06, Volume: 40, Issue:9 Topics: Amino Acid Substitution; Animals; Arginase; Arginine; Binding, Competitive; Catalysis; Crystallography, X-Ray; Cysteine; Enzyme Inhibitors; Histidine; Macromolecular Substances; Models, Molecular; Mutagenesis, Site-Directed; Ornithine; Rats; Recombinant Proteins; Structure-Activity Relationship; Substrate Specificity; Urea	2001

Article

Year

L-arginine binding to liver arginase requires proton transfer to gateway residue His141 and coordination of the guanidinium group to the dimanganese(II,II) center.

Biochemistry, 1998, Jun-09, Volume: 37, Issue:23

Topics: Animals; Arginase; Arginine; Asparagine; Binding Sites; Borates; Citrulline; Electron Spin Resonance Spectroscopy; Guanidine; Histidine; Hydrogen-Ion Concentration; Isoleucine; Liver; Lysine; Manganese; Mutagenesis, Site-Directed; Ornithine; Protons; Rats; Substrate Specificity

1998

Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase.

Biochemistry, 2001, Mar-06, Volume: 40, Issue:9

Topics: Amino Acid Substitution; Animals; Arginase; Arginine; Binding, Competitive; Catalysis; Crystallography, X-Ray; Cysteine; Enzyme Inhibitors; Histidine; Macromolecular Substances; Models, Molecular; Mutagenesis, Site-Directed; Ornithine; Rats; Recombinant Proteins; Structure-Activity Relationship; Substrate Specificity; Urea

2001