Mechanism of the myo-inositol phosphatase reaction

Janis K. Shute; Raymond Baker; David C. Billington; David Gani

doi:10.1039/C39880000422

Mechanism of the myo-inositol phosphatase reaction

Janis K. Shute
, Raymond Baker
, David C. Billington
, David Gani^*

^*Corresponding author for this work

Institute of Life Sciences and Healthcare

Merck

Research output: Contribution to journal › Article › peer-review

Abstract

myo-Inositol phosphatase from bovine brain operates via a ping-pong mechanism whereby phosphate is transferred from the substrate to the enzyme and then from the enzyme to water; lithium cation inhibits the second step.

Original language	English
Pages (from-to)	422-423
Number of pages	2
Journal	Journal of the Chemical Society, Chemical Communications
Issue number	6
DOIs	https://doi.org/10.1039/C39880000422
Publication status	Published - 1 Jan 1988

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title = "Mechanism of the myo-inositol phosphatase reaction",

abstract = "myo-Inositol phosphatase from bovine brain operates via a ping-pong mechanism whereby phosphate is transferred from the substrate to the enzyme and then from the enzyme to water; lithium cation inhibits the second step.",

author = "Shute, \{Janis K.\} and Raymond Baker and Billington, \{David C.\} and David Gani",

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AB - myo-Inositol phosphatase from bovine brain operates via a ping-pong mechanism whereby phosphate is transferred from the substrate to the enzyme and then from the enzyme to water; lithium cation inhibits the second step.

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JO - Journal of the Chemical Society, Chemical Communications

JF - Journal of the Chemical Society, Chemical Communications

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Mechanism of the myo-inositol phosphatase reaction

Abstract

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