Chemical Modification and Site-Directed Mutagenesis of Human Liver Arginase: Evidence That the Imidazole Group of Histidine-141 Is Not Involved in Substrate Binding
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference26 articles.
1. Nuclear Magnetic Resonance Studies of Manganese Binding of Rat Liver Arginase
2. EPR evidence for binuclear manganese(II) centers in rat liver arginase
3. Interaction of arginase with metal ions: studies of the enzyme from human liver and comparison with other arginases
4. Purification of Human Hepatic Arginase and Its Manganese (II)-Dependent and pH-Dependent Interconversion between Active and Inactive Forms: A Possible pH-Sensing Function of the Enzyme on the Ornithine Cycle
5. Structure of a unique binuclear manganese cluster in arginase
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1. Enzyme Cascade with Horseradish Peroxidase Readout for High-Throughput Screening and Engineering of Human Arginase-1;Analytical Chemistry;2023-04-24
2. Identification of agmatinase from Vibrio splendidus and its roles in modulating arginine metabolism of Apostichopus japonicus;Aquaculture;2018-07
3. Homoarginine and inhibition of human arginase activity: kinetic characterization and biological relevance;Scientific Reports;2018-02-27
4. Arginase Inhibitors: A Rational Approach Over One Century;Medicinal Research Reviews;2016-11-15
5. Structure and Function of Non-Native Metal Clusters in Human Arginase I;Biochemistry;2012-10-12
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