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Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
J Biol Chem. 2015 Jul 10;290(28):17576-86. doi: 10.1074/jbc.M115.659680. Epub 2015 May 26.
J Biol Chem. 2015.
PMID: 26013825
Free PMC article.
Characterization of Helicobacter pylori gamma-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis.
Morrow AL, Williams K, Sand A, Boanca G, Barycki JJ.
Morrow AL, et al.
Biochemistry. 2007 Nov 20;46(46):13407-14. doi: 10.1021/bi701599e. Epub 2007 Oct 26.
Biochemistry. 2007.
PMID: 17960917
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