Zobrazeno 1 - 10
of 97
pro vyhledávání: '"Christopher C. Lawrence"'
Publikováno v:
Journal of the American Chemical Society. 121:7463-7468
Ribonucleoside triphosphate reductase (RTPR) from Lactobacillus leichmannii catalyzes the reduction of nucleotides to deoxynucleotides with concomitant oxidation of two cysteines within the active site to a disulfide. RTPR requires adenosylcobalamin
Autor:
János Rétey, JoAnne Stubbe, Gary J. Gerfen, Rainer Nitsche, Christopher C. Lawrence, Vicente Samano, Morris J. Robins
Publikováno v:
Journal of Biological Chemistry. 274:7039-7042
The ribonucleoside triphosphate reductase (RTPR) from Lactobacillus leichmannii catalyzes the reduction of nucleoside 5′-triphosphates to 2′-deoxynucleoside 5′-triphosphates and uses coenzyme B12, adenosylcobalamin (AdoCbl), as a cofactor. Use
Autor:
Christopher C. Lawrence, JoAnne Stubbe
Publikováno v:
Current Opinion in Chemical Biology. 2:650-655
Ribonucleoside triphosphate reductase from Lactobacillus leichmannii catalyzes the reduction of nucleotides to deoxynucleotides and uses adenosylcobalamin as a cofactor. transient protein-based thiyl radical is essential for catalysis. Studies direct
Publikováno v:
Tetrahedron. 53:12005-12016
Ribonucleotide reductases catalyze the reduction of nucleotides to deoxynucleotides in all organisms. 2′-Ara-2′-azido-2′-deoxyadenosin-5′-triphosphate (araN 3 ATP) is a potent mechanism based inhibitor of the AdoCbl-dependent enzyme from Lact
Autor:
Victor Lee, Christopher J. Schofield, J. Kenneth Robinson, Jack E. Baldwin, Robert A. Field, Christopher C. Lawrence
Publikováno v:
Tetrahedron Letters. 35:4649-4652
The substrate specificity of L -proline-4-hydroxylase, a 2-oxoglutarate dependent dioxygenase from Streptomyces griseoviridus P8648, was investigated. Preliminary assays measuring turnover of 2-oxoglutarate indicated 3,4-dehydro- L -proline was an ef
Autor:
Jack E. Baldwin, Christopher J. Schofield, Christopher C. Lawrence, J. K. Robinson, Robert A. Field, Victor Lee
Publikováno v:
ChemInform. 25
Publikováno v:
ChemInform. 28
Ribonucleotide reductases catalyze the reduction of nucleotides to deoxynucleotides in all organisms. 2′-Ara-2′-azido-2′-deoxyadenosin-5′-triphosphate (araN 3 ATP) is a potent mechanism based inhibitor of the AdoCbl-dependent enzyme from Lact
Publikováno v:
Langmuir : the ACS journal of surfaces and colloids. 20(11)
Structural investigations of bare and surface-modified polystyrene microspheres (beads) have been carried out by infrared-visible sum frequency generation (SFG) vibrational spectroscopy and scanning force microscopy (SFM). Bead surfaces have been mod
Autor:
Honorio V. Obias, Robert G. Griffin, Galit Bar, JoAnne Stubbe, Christopher C. Lawrence, Marina Bennati
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 96(16)
Class I ribonucleotide reductases (RNRs) are composed of two subunits, R1 and R2. The R2 subunit contains the essential diferric cluster–tyrosyl radical (Y⋅) cofactor and R1 is the site of the conversion of nucleoside diphosphates to 2′-deoxynu
Publikováno v:
Biochemistry. 38(4)
In the catalytic mechanism of nucleotide reduction, ribonucleoside triphosphate reductase (RTPR) from Lactobacillus leichmannii catalyzes the homolytic cleavage of the carbon-cobalt bond of adenosylcobalamin (AdoCbl) at a rate approximately 10(11)-fo