(Q27617591)

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A model of the transition state in the alkaline phosphatase reaction

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A model of the transition state in the alkaline phosphatase reaction (English)

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author name string

K M Holtz

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1

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B Stec

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2

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E R Kantrowitz

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3

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language of work or name

English

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publication date

26 March 1999

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published in

Journal of Biological Chemistry

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volume

274

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page(s)

8351-4

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issue

13

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cites work

Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis

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21 January 2018

Nuclear magnetic resonance and neutron diffraction studies of the complex of ribonuclease A with uridine vanadate, a transition-state analogue

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21 January 2018

Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism

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21 January 2018

A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase

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21 January 2018

Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases

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21 January 2018

Vanadium ion inhibition of alkaline phosphatase-catalyzed phosphate ester hydrolysis

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21 January 2018

SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

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21 January 2018

Trapping and visualization of a covalent enzyme-phosphate intermediate

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retrieved

21 January 2018

Function of arginine-166 in the active site of Escherichia coli alkaline phosphatase

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reference URL

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21 January 2018

Identifiers

DOI

10.1074/JBC.274.13.8351

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PubMed ID

10085061

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ResearchGate publication ID

13206149

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(Q27617591)

A model of the transition state in the alkaline phosphatase reaction

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