Literature DB >> 4968184

Studies on the nature of the binding of thiamine pyrophosphate to enzymes.

A V Morey, E Juni.   

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Year:  1968        PMID： 4968184

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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  6 in total

1.  Inhibition of thiamine pyrophosphate utilization by thiamine or its monophosphate in Escherichia coli.

Authors:  H Nakayama; R Hayashi
Journal:  J Bacteriol       Date:  1974-04       Impact factor: 3.490

2.  Pyruvate Decarboxylase from Zea mays L. : I. Purification and Partial Characterization from Mature Kernels and Anaerobically Treated Roots.

Authors:  T C Lee; P J Langston-Unkefer
Journal:  Plant Physiol       Date:  1985-09       Impact factor: 8.340

3.  Pyruvate decarboxylase from Zymomonas mobilis. Structure and re-activation of apoenzyme by the cofactors thiamin diphosphate and magnesium ion.

Authors:  R J Diefenbach; R G Duggleby
Journal:  Biochem J       Date:  1991-06-01       Impact factor: 3.857

4.  Pyruvate Decarboxylase from Zea mays L. : 2. Examination of Hysteretic Kinetics.

Authors:  P J Langston-Unkefer; T C Lee
Journal:  Plant Physiol       Date:  1985-10       Impact factor: 8.340

5.  Conditions for the self-catalysed inactivation of carnitine acetyltransferase. A novel form of enzyme inhibition.

Authors:  J F Chase; P K Tubbs
Journal:  Biochem J       Date:  1969-01       Impact factor: 3.857

6.  Staphylococcus aureus CidC Is a Pyruvate:Menaquinone Oxidoreductase.

Authors:  Xinyan Zhang; Kenneth W Bayles; Sorin Luca
Journal:  Biochemistry       Date:  2017-08-25       Impact factor: 3.162
  6 in total

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