A Carbon-Centred Alkylphosphonate Radical Generated by Pyruvate Formate-Lyase with its Substrate Analogue Hypophosphite

1988 ◽  
pp. 141-142 ◽  
Author(s):  
Volker Unkrig ◽  
Joachim Knappe ◽  
Franz A. Neugebauer
Keyword(s):  
Pyruvate Formate Lyase ◽  
Substrate Analogue

Pyruvate Formate Lyase:  A New Perspective

2003 ◽  
Vol 107 (24) ◽  
pp. 5751-5757 ◽  
Author(s):  
Maria de Fátima Lucas ◽  
Pedro Alexandrino Fernandes ◽  
Leif A. Eriksson ◽  
Maria João Ramos
Keyword(s):  
Pyruvate Formate Lyase ◽  
New Perspective

Rescuing of the hydride transfer reaction in the Glu312Asp variant of choline oxidase by a substrate analogue

2010 ◽  
Vol 499 (1-2) ◽  
pp. 1-5 ◽  
Author(s):  
Osbourne Quaye ◽  
Tranbao Nguyen ◽  
Swathi Gannavaram ◽  
Andrea Pennati ◽  
Giovanni Gadda
Keyword(s):  
Transfer Reaction ◽  
Hydride Transfer ◽  
Choline Oxidase ◽  
Substrate Analogue ◽  
Hydride Transfer Reaction

scholarly journals Identification and Analysis of Genes Involved in Anaerobic Toluene Metabolism by Strain T1: Putative Role of a Glycine Free Radical

1998 ◽  
Vol 64 (5) ◽  
pp. 1650-1656 ◽  
Author(s):  
Peter W. Coschigano ◽  
Thomas S. Wehrman ◽  
L. Y. Young
Keyword(s):  
Free Radical ◽  
Amino Acid ◽  
Molecular Mass ◽  
Cysteine Residue ◽  
Open Reading Frames ◽  
Site Directed Mutagenesis ◽  
Pyruvate Formate Lyase ◽  
Calculated Molecular Mass ◽  
Acid Protein ◽  
Amino Acid Protein

ABSTRACT The denitrifying strain T1 is able to grow with toluene serving as its sole carbon source. Two mutants which have defects in this toluene utilization pathway have been characterized. A clone has been isolated, and subclones which contain tutD and tutE, two genes in the T1 toluene metabolic pathway, have been generated. ThetutD gene codes for an 864-amino-acid protein with a calculated molecular mass of 97,600 Da. The tutE gene codes for a 375-amino-acid protein with a calculated molecular mass of 41,300 Da. Two additional small open reading frames have been identified, but their role is not known. The TutE protein has homology to pyruvate formate-lyase activating enzymes. The TutD protein has homology to pyruvate formate-lyase enzymes, including a conserved cysteine residue at the active site and a conserved glycine residue that is activated to a free radical in this enzyme. Site-directed mutagenesis of these two conserved amino acids shows that they are also essential for the function of TutD.

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