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  • 1
    Electronic Resource
    Electronic Resource
    Kinetics of Inhibition of Green Crab (Scylla Serrata) Alkaline Phosphatase by Sodium (2,2′-bipyridine) Oxodiperoxovanadate (1999)
    Springer
    The protein journal 18 (1999), S. 735-740 
    Details
    ISSN: 1573-4943
    Keywords: Alkaline phosphatase ; sodium (2, 2′-bipyridine) oxodiperoxovanadate ; inhibition ; kinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Green crab (Scylla serrata) alkaline phosphatase (EC 3.1.3.1) is a metalloenzyme, which catalyzes the nonspecific hydrolysis of phosphate monoesters. The kinetics of inhibition of the enzyme by sodium (2, 2′-bipyridine) oxodiperoxovanadate, pV(bipy), has been studied. The time course of the hydrolysis of p-nitrophenyl-phosphate catalyzed by the enzyme in the presence of different pV(bipy) concentrations showed that at each pV(bipy) concentration, the rate decreased with increasing time until a straight line was approached, the straight line slopes are the same for all concentrations. The results suggest that the inhibition of the enzyme by pV(bipy) is a slow, reversible reaction with fractional remaining activity. The microscopic rate constants are determined for the reaction of inhibitor with the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020621332377
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  • 2
    Electronic Resource
    Electronic Resource
    Kinetics of inhibition of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide (1996)
    Springer
    The protein journal 15 (1996), S. 345-350 
    Details
    ISSN: 1573-4943
    Keywords: Alkaline phosphatase ; inhibition ; chemical modification ; N-bromosuccinimide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The inactivation of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide has been studied using the kinetic method of the substrate reaction during modification of enzyme activity previously described by Tsou [(1988),Adv. Enzymol. Related Areas Mol. Biol. 61, 381–436]. The results show that inactivation of the enzyme is a slow, reversible reaction. The microscopic rate constants for the reaction of the inactivator with free enzyme and the enzyme-substrate complex were determined. Comparison of these rate constants indicates that the presence of substrate offers marked protection of this enzyme against inactivation by N-bromosuccinimide. The above results suggest that the tryptophan residue is essential for activity and is situated at the active site of the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01886860
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  • 3
    Electronic Resource
    Electronic Resource
    Comparison of inactivation and unfolding of green crab (Scylla serrata) alkaline phosphatase during denaturation by guanidinium chloride (1996)
    Springer
    The protein journal 15 (1996), S. 359-365 
    Details
    ISSN: 1573-4943
    Keywords: Alkaline phosphatase ; denaturation ; inactivation ; guanidinium chloride
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Green crab (Scylla serrata) alkaline phosphatase (EC 3.1.3.1) is a metalloenzyme, each active site in which contains a tight cluster of two zinc ions and one magnesium ion. Unfolding and inactivation of the enzyme during denaturation in guanidinium chloride (GuHCl) solutions of different concentrations have been compared. The kinetic theory of the substrate reaction during irreversible inhibition of enzyme activity previously described by Tsou [(1988),Adv. Enzymol. Related Areas Mol. Biol. 61, 381–436] has been applied to a study on the kinetics of the course of inactivation of the enzyme during denaturation by GuHCl. The rate constants of unfolding and inactivation have been determined. The results show that inactivation occurs before noticeable conformational change can be detected. It is suggested that the active site of green crab alkaline phosphatase containing multiple metal ions is also situated in a limited region of the enzyme molecule that is more fragile to denaturants than the protein as a whole.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01886862
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  • 4
    Electronic Resource
    Electronic Resource
    Kinetics of Inhibition of Green Crab (Scylla serrata) Alkaline Phosphatase by L-Cysteine (1999)
    Springer
    The protein journal 18 (1999), S. 603-607 
    Details
    ISSN: 1573-4943
    Keywords: Alkaline phosphatase ; green crab ; inhibition ; kinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The inhibition of alkaline phosphatase from green crab (Scylla serrata) by L-cysteine has been studied. The results show that L-cysteine gives a mixed-type inhibition. The progress-of-substrate-reaction method previously described by Tsou [(1988), Adv. Enzymol. Related Areas Mol. Biol. 61, 391–436] was used to study the inactivation kinetics of the enzyme by L-cysteine. The microscopic rate constants were determined for reaction of the inhibitor with the free enzyme and the enzyme–substrate complex (ES) The results show that inactivation of the enzyme by L-cysteine is a slow, reversible reaction. Comparison of the inactivation rate constants of free enzyme and ES suggests that the presence of the substrate offers marked protection of this enzyme against inactivation by L-cysteine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020611602818
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