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Found 31 results
Filters: keyword is Catalysis [Clear All Filters]
2007
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2007. The crystal structure of phenylpyruvate decarboxylase from Azospirillum brasilense at 1.5 A resolution. Implications for its catalytic and regulatory mechanism.
FEBS J. 274(9):2363-2375. Abstract
2006
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2006. Interplay between ion binding and catalysis in the thioredoxin-coupled arsenate reductase family.
J. Mol. Biol.. 360(4):826-838. Abstract
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2006. Transition-state complex of the purine-specific nucleoside hydrolase of T. vivax: enzyme conformational changes and implications for catalysis.
Journal Molecular Biology. 359(2):331-346. Abstract
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2006. The activation of electrophile, nucleophile and leaving group during the reaction catalysed by pI258 arsenate reductase.
Chembiochem.. 7(6):981-989. Abstract
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2006. Pathways of disulfide bond formation in Escherichia coli.
Int. J. Biochem. Cell Biol.. 38(7):1050-1062. Abstract
2005
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2005. Substrate-assisted leaving group activation in enzyme-catalyzed N-glycosidic bond cleavage.
J. Biol. Chem. 280(15):14799-14802. Abstract
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2005. Encapsulation of therapeutic nucleoside hydrolase in functionalised nanocapsules.
J Control Release. 102(1):171-179. Abstract
2004
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2004. Leaving group activation by aromatic stacking: an alternative to general acid catalysis.
J. Mol. Biol. 338(1):1-6. Abstract
2003
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2003. Catalysis by nucleoside hydrolases.
Current opinion in structural biology. 13(6):731-738. Abstract
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2003. Ribonucleases: from prototypes to therapeutic targets?.
Current Medicinal Chemistry. 10(9):779-785. Abstract
2002
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2002. All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade.
Proc. Natl. Acad. Sci. USA. 99(13):8506-8511. Abstract
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2002. Enzyme-substrate interactions in the purine-specific nucleoside hydrolase from Trypanosoma vivax.
J. Biol. Chem. 277(18):15938-15946. Abstract
2001
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2001. Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty.
Nat. Struct. Biol.. 8(10):843-847. Abstract
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2001. Deciphering the mechanism of RNase T1.
341:305-323.
2000
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2000. Mechanism of RNase T1: concerted triester-like phosphoryl transfer via a catalytic three-centered hydrogen bond.
7(8):651-658. Abstract
1999
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1999. The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus.
Biochemistry. 38(51):16857-16865. Abstract
1998
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1998. Reconsidering the energetics of ribonuclease catalysed RNA hydrolysis.
257(1):286-290. Abstract
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1998. Reconsidering the energetics of ribonuclease catalysed RNA hydrolysis.
257(1):286-290. Abstract
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1998. An engineered ribonuclease preferring phosphorothioate RNA.
5(5):365-368. Abstract
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1998. Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.
273(4):2199-2206. Abstract
1996
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1996. A catalytic function for the structurally conserved residue Phe 100 of ribonuclease T1.
5(8):1523-1530. Abstract
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1996. A catalytic function for the structurally conserved residue Phe 100 of ribonuclease T1.
5(8):1523-1530. Abstract
1994
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1994. Investigation of the functional interplay between the primary site and the subsite of RNase T1: kinetic analysis of single and multiple mutants for modified substrates.
18(4):318-323. Abstract
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1994. Investigation of the functional interplay between the primary site and the subsite of RNase T1: kinetic analysis of single and multiple mutants for modified substrates.
18(4):318-323. Abstract
1993