• Publications
  • Influence
Human P450 metabolism of warfarin.
TLDR
The anticoagulant drug warfarin occurs as a pair of enantiomers that are differentially metabolized by human cytochromes P450 (CYP) and is affected primarily when metabolism of S-warfarin is altered. Expand
Protein tyrosine phosphatases: prospects for therapeutics.
  • Z. Zhang
  • Biology, Medicine
  • Current opinion in chemical biology
  • 1 August 2001
TLDR
Significant progress has been made in identifying small molecules that simultaneously bind both the active site and a unique adjacent site that enables specific inhibition of individual PTP isoenzymes, suggesting that PTP inhibitors may ultimately serve as powerful therapeutic weapons in the authors' arsenal for battling human diseases. Expand
Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis.
  • Z. Zhang
  • Biology, Medicine
  • Critical reviews in biochemistry and molecular…
  • 1998
TLDR
Biochemical experiments demonstrate that phosphatases in the PTPase superfamily utilize a common mechanism for catalysis going through a covalent thiophosphate intermediate that involves the nucleophilic Cys residue in thePTPase signature motif. Expand
Mutational analysis of the catalytic subunit of muscle protein phosphatase-1.
TLDR
The results of the mutational analysis of rabbit skeletal muscle protein phosphatase-1 are consistent with the involvement of conserved His and Asp residues in metal binding, and are discussed in the context of the recently described crystal structure of PP1, which reveals that PP1 possesses a bimetallic center at the active site. Expand
Control of cationic amino acid transport and retroviral receptor functions in a membrane protein family.
TLDR
Results demonstrate that domains of these transporters can function in chimeric combinations to control viral receptor and transport functions. Expand
Tyrosine-272 is involved in the inhibition of protein phosphatase-1 by multiple toxins.
TLDR
The studies show that Tyr-272 is of specific importance for the binding of these inhibitors and provide strong evidence for the postulate that these toxins all bind to a common inhibitor site on PP1. Expand
Characterization of human cytochromes P450 involved in theophylline 8-hydroxylation.
TLDR
Correlations of rates of theophylline 8-hydroxylation to 1,3-DU with other P450 form-specific activities, in a series of ten human liver microsomal preparations, revealed that at low concentrations the metabolism was catalyzed primarily by P4501A2, while at high substrate concentrations P4502E1 was primarily responsible for catalysis. Expand
Characterization of purified human recombinant cytochrome P4501A1-Ile462 and -Val462: assessment of a role for the rare allele in carcinogenesis.
TLDR
With the carcinogen benzo(a) pyrene as substrate, reconstituted CYP1A1-Ile462 together with epoxide hydrolase produced 7,8- and 9,10-dihydrodiols at comparable rates than did CYP 1A 1-Val462, probably not related to greater extents of carcinogen bioactivation. Expand
Kinetic and mechanistic characterization of a mammalian protein- tyrosine phosphatase, PTP1
  • Z. Zhang
  • Chemistry, Medicine
  • The Journal of Biological Chemistry
  • 1 May 1995
TLDR
The leaving group dependence of kcat/Km suggests that there is a strong electrophilic interaction between the enzyme and the leaving group oxygen in the transition state of the phosphorylation event, suggesting that the mechanism for PTPase-catalyzed phosphate monoester hydrolysis is conserved from bacterial to mammals. Expand
Are protein-tyrosine phosphatases specific for phosphotyrosine?
  • Z. Zhang
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • 7 July 1995
TLDR
It is demonstrated here that both the Yersinia PTPase and rat PTP1 can dephosphorylate alkyl phosphates such as flavin mononucleotide, pyridoxal 5'-phosphate, D-glucose 6-ph phosphate, DL-alpha-glycerophosphate , and O-phospho-L-serine, reflecting the intrinsic lower chemical reactivity of the alkyL phosphates. Expand
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