Literature DB >> 8185582

Enzyme kinetics of lipolysis revisited: the role of lipase interfacial binding.

A G Marangoni1.   

Abstract

A model for the enzyme kinetics of lipolysis was developed where the rate limiting step of the reaction is the interfacial binding step. Binding involves the association of the enzyme with a cluster of substrate molecules and a conformational change in the enzyme, resulting in an interfacially penetrated lipase bound to a cluster of substrate molecules. The resulting derived rate equation is identical to the HIll equation. Fits of the model to experimental velocity vs. substrate concentration data from the literature allowed for the determination of enzyme-substrate interface dissociation constants and reaction order with respect to substrate concentration.

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Year:  1994        PMID: 8185582     DOI: 10.1006/bbrc.1994.1595

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  Substrate binding in the processive cellulase Cel7A: Transition state of complexation and roles of conserved tryptophan residues.

Authors:  Nanna Røjel; Jeppe Kari; Trine Holst Sørensen; Silke F Badino; J Preben Morth; Kay Schaller; Ana Mafalda Cavaleiro; Kim Borch; Peter Westh
Journal:  J Biol Chem       Date:  2019-12-17       Impact factor: 5.157

2.  Selective mobilization of fatty acids from white fat cells: evidence for a relationship to the polarity of triacylglycerols.

Authors:  T Raclot
Journal:  Biochem J       Date:  1997-03-01       Impact factor: 3.857

Review 3.  Protein engineering and applications of Candida rugosa lipase isoforms.

Authors:  Casimir C Akoh; Guan-Chiun Lee; Jei-Fu Shaw
Journal:  Lipids       Date:  2004-06       Impact factor: 1.880

  3 in total

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