Inhibition of protein tyrosine phosphatases by low-molecular-weight S-nitrosothiols and S-nitrosylated human serum albumin

Ming Xian, Kun Wang, Xinchao Chen, Yongchun Hou, Andrea McGill, Xi Chen, Bo Zhou, Zhong Yin Zhang, Jin Pei Cheng, Peng George Wang

Research output: Contribution to journalArticle

32 Scopus citations


The homogeneous recombinant mammalian protein tyrosine phosphatase 1B (PTP1B) and Yersinia protein tyrosine phosphatase (PTPase) are inactivated by a series of low-molecular-weight S-nitrosothiols. These compounds exhibited different inhibitory activities in a time- and concentration-dependent manner with second-order rate constants (k(inact)/K(I)) ranging from 37 to 113 M-1 min-1 against mammalian PTP1B and from 66 to 613 M-1 min-1 against Yersinia PTPase. Furthermore, the inactivation of Yersinia PTPase by S-nitrosylated protein:S-nitroso human serum albumin was investigated. Both single-S-nitrosylated and poly-S-nitrosylated human serum albumin show good inhibitory ability to Yersinia PTPase. The second-order rate constants are 472 and 1188 M-1 min-1, respectively. This result indicates a possibility that S-nitrosylated albumin in vivo may function as an inhibitor for a variety of cysteine-dependent enzymes. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)310-314
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Feb 16 2000
Externally publishedYes



  • Inhibition
  • Nitric oxide
  • Protein tyrosine phosphatases
  • S-nitrosothiols
  • S-nitrosylated human serum albumin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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