Calf spleen purine nucleoside phosphorylase: complex kinetic mechanism, hydrolysis of 7-methylguanosine, and oligomeric state in solution (Q43990804)

28 November 2017

title

Calf spleen purine nucleoside phosphorylase: complex kinetic mechanism, hydrolysis of 7-methylguanosine, and oligomeric state in solution (English)

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28 November 2017

Agnieszka Bzowska

1

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28 November 2017

publication date

1 April 2002

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Biochimica et Biophysica Acta

28 November 2017

published in

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28 November 2017

volume

1596

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28 November 2017

issue

2

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28 November 2017

page(s)

293-317

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Purine nucleoside phosphorylases: properties, functions, and clinical aspects

28 November 2017

cites work

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Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis

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Allosteric regulation of purine nucleoside phosphorylase.

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Calf spleen purine nucleoside phosphorylase: purification, sequence and crystal structure of its complex with an N(7)‐acycloguanosine inhibitor

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7 January 2021

Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15 A resolution

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Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (Sulphate) at 2.1 A resolution

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Crystal structure of the purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implication for the mechanism of trimeric PNPs

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The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology

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Calf spleen purine nucleoside phosphorylase complexed with substrates and substrate analogues

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Purine nucleoside phosphorylase: its use in a spectroscopic assay for inorganic phosphate and for removing inorganic phosphate with the aid of phosphodeoxyribomutase

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Purine nucleoside phosphorylase. 2. Catalytic mechanism

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Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism

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An improved assay for nanomole amounts of inorganic phosphate

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Purine nucleoside phosphorylase: inhibition by purine N(7)- and N(9)-acyclonucleosides; and substrate properties of 7-beta-D-ribofuranosylguanine and 7-beta-D-ribofuranosylhypoxanthine

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72 Purine nucleoside phosphorylase from human erythrocytes

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Properties of two unusual, and fluorescent, substrates of purine-nucleoside phosphorylase: 7-methylguanosine and 7-methylinosine

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Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin

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Purine nucleoside phosphorylase. Inosine hydrolysis, tight binding of the hypoxanthine intermediate, and third-the-sites reactivity

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Purine nucleoside phosphorylase. VI. Microheterogeneity and comparison of kinetic behavior of the enzyme from several tissues and species

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Calf spleen purine nucleoside phosphorylase: structure of its ternary complex with an N(7)-acycloguanosine inhibitor and a phosphate anion

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Deviations from Michaelis-Menten kinetics. The possibility of complicated curves for simple kinetic schemes and the computer fitting of experimental data for acetylcholinesterase, acid phosphatase, adenosine deaminase, arylsulphatase, benzylamine ox

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Simple enzyme kinetic mechanisms that can give all possible velocity profiles with chemically reasonable rate constant values

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Dose any enzyme follow the Michaelis-Menten equation?

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Crystallization and some properties of purine nucleoside phosphorylase from chicken liver

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Design of an adenosine phosphorylase by active-site modification of murine purine nucleoside phosphorylase. Enzyme kinetics and molecular dynamics simulation of Asn-243 and Lys-244 substitutions of purine nucleoside phosphorylase

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Identifiers

DOI

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28 November 2017

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