The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein (Q22010421)

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Language	Label	Description	Also known as
English	The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein	scientific article

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scholarly article

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The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein (English)

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Saccharomyces cerevisiae

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P(1),P(6)-bis(5'-adenosyl)hexaphosphate

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ChEBI release 2020-05-28

Nudix hydrolase 3

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GOA release 2020-03-11

diadenosine polyphosphate catabolic process

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GOA release 2020-03-11

Polyphosphatase DDP1 YOR163W

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GOA release 2020-03-11

Schizosaccharomyces pombe

object named as

Schizosaccharomyces pombe

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based on heuristic

inferred from title

author name string

S T Safrany

1

author given names

S T

author last names

Safrany

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PubMed publication ID

7 February 2023

S W Ingram

2

author given names

S W

author last names

Ingram

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PubMed publication ID

7 February 2023

J L Cartwright

3

author given names

J L

author last names

Cartwright

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PubMed publication ID

7 February 2023

J R Falck

4

author given names

J R

author last names

Falck

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PubMed publication ID

7 February 2023

A G McLennan

5

author given names

A G

author last names

McLennan

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PubMed publication ID

7 February 2023

L D Barnes

6

author given names

L D

author last names

Barnes

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PubMed publication ID

7 February 2023

S B Shears

7

author given names

S B

author last names

Shears

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PubMed publication ID

7 February 2023

language of work or name

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publication date

30 July 1999

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Journal of Biological Chemistry

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274

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31

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21735-40

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1 reference

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10.1074/JBC.274.31.21735

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