Literature DB >> 11342026

Inhibition kinetics of green crab (Scylla serrata) alkaline phosphatase by zinc ions: a new type of complexing inhibition.

R Q Zhang1, Q X Chen, R Xiao, L P Xie, X G Zeng, H M Zhou.   

Abstract

The Tsou method was used to study the kinetic course of inactivation of green crab alkaline phosphatase by zinc ions. The results show that the enzyme was inactivated by a complexing scheme which has not been previously identified. The enzyme first reversibly and quickly binds Zn(2+) and then undergoes a slow reversible course to inactivation and slow conformational change. The inactivation reaction is a single molecule reaction and the apparent inactivation rate constant is for a saturated reaction being independent of Zn(2+) concentration if the concentration is sufficiently high. The microscopic rate constants of inactivation and the association constant were determined from the measurements.

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Year:  2001        PMID: 11342026     DOI: 10.1016/s0167-4838(00)00254-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  A PPM-family protein phosphatase from the thermoacidophile Thermoplasma volcanium hydrolyzes protein-bound phosphotyrosine.

Authors:  Hanan Dahche; Abdulshakur Abdullah; M Ben Potters; Peter J Kennelly
Journal:  Extremophiles       Date:  2008-11-29       Impact factor: 2.395

2.  Inactivation kinetics of mushroom tyrosinase by cetylpyridinium chloride.

Authors:  Qing-Xi Chen; Huang Huang; Isao Kubo
Journal:  J Protein Chem       Date:  2003-07
  2 in total

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