Stereochemical Course of the Reaction Catalyzed by 5‘-Nucleotide Phosphodiesterase from Snake Venom

Floyd R. Bryant; Stephen J. Benkovic

doi:10.1021/bi00580a022

Stereochemical Course of the Reaction Catalyzed by 5‘-Nucleotide Phosphodiesterase from Snake Venom

Floyd R. Bryant, Stephen J. Benkovic

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127 Scopus citations

Abstract

The hydrolysis reaction of ATPαS by snake venom phosphodiesterase is highly specific for the B diastereomer and proceeds with 88% retention of configuration at phosphorus. Since this enzyme also catalyzes the hydrolysis of the S enantiomer of O-p-nitrophenyl phenylphosphonothioate, the absolute configuration at Pα of ATPαS (B) is assigned as the R configuration provided the two substrates are processed identically. A mechanism for the hydrolysis reactions catalyzed by the venom phosphodiesterase involving at least a single covalent phosphoryl-enzyme intermediate is in accord with this result.

Original language	English (US)
Pages (from-to)	2825-2828
Number of pages	4
Journal	Biochemistry
Volume	18
Issue number	13
DOIs	https://doi.org/10.1021/bi00580a022
State	Published - 1979
Externally published	Yes

ASJC Scopus subject areas

Biochemistry

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10.1021/bi00580a022

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title = "Stereochemical Course of the Reaction Catalyzed by 5{\textquoteleft}-Nucleotide Phosphodiesterase from Snake Venom",

abstract = "The hydrolysis reaction of ATPαS by snake venom phosphodiesterase is highly specific for the B diastereomer and proceeds with 88% retention of configuration at phosphorus. Since this enzyme also catalyzes the hydrolysis of the S enantiomer of O-p-nitrophenyl phenylphosphonothioate, the absolute configuration at Pα of ATPαS (B) is assigned as the R configuration provided the two substrates are processed identically. A mechanism for the hydrolysis reactions catalyzed by the venom phosphodiesterase involving at least a single covalent phosphoryl-enzyme intermediate is in accord with this result.",

author = "Bryant, {Floyd R.} and Benkovic, {Stephen J.}",

year = "1979",

doi = "10.1021/bi00580a022",

language = "English (US)",

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journal = "Biochemistry",

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AU - Bryant, Floyd R.

AU - Benkovic, Stephen J.

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N2 - The hydrolysis reaction of ATPαS by snake venom phosphodiesterase is highly specific for the B diastereomer and proceeds with 88% retention of configuration at phosphorus. Since this enzyme also catalyzes the hydrolysis of the S enantiomer of O-p-nitrophenyl phenylphosphonothioate, the absolute configuration at Pα of ATPαS (B) is assigned as the R configuration provided the two substrates are processed identically. A mechanism for the hydrolysis reactions catalyzed by the venom phosphodiesterase involving at least a single covalent phosphoryl-enzyme intermediate is in accord with this result.

AB - The hydrolysis reaction of ATPαS by snake venom phosphodiesterase is highly specific for the B diastereomer and proceeds with 88% retention of configuration at phosphorus. Since this enzyme also catalyzes the hydrolysis of the S enantiomer of O-p-nitrophenyl phenylphosphonothioate, the absolute configuration at Pα of ATPαS (B) is assigned as the R configuration provided the two substrates are processed identically. A mechanism for the hydrolysis reactions catalyzed by the venom phosphodiesterase involving at least a single covalent phosphoryl-enzyme intermediate is in accord with this result.

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JO - Biochemistry

JF - Biochemistry

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Stereochemical Course of the Reaction Catalyzed by 5‘-Nucleotide Phosphodiesterase from Snake Venom

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