Literature DB >> 5101632

Tyrosyl and lysyl residues involved in the reactivity of catalytic and regulatory sites of crystalline beef liver glutamate dehydrogenase.

G Di Prisco.   

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Year:  1971        PMID： 5101632     DOI： 10.1021/bi00780a007

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  3 in total

1.  The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal5'-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity.

Authors:  S S Chen; P C Engel
Journal:  Biochem J       Date:  1975-05       Impact factor: 3.857

2.  The significance of abrupt transitions in Lineweaver-Burk plots with particular reference to glutamate dehydrogenase. Negative and positive co-operativity in catalytic rate constants.

Authors:  P C Engel; W Ferdinand
Journal:  Biochem J       Date:  1973-01       Impact factor: 3.857

3.  The binding of oxidized coenzymes by glutamate dehydrogenase and the effects of glutarate and purine nucleotides.

Authors:  K Dalziel; R R Egan
Journal:  Biochem J       Date:  1972-02       Impact factor: 3.857
  3 in total

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