(Q22010877)

English

Site-directed mutagenesis of diphosphoinositol polyphosphate phosphohydrolase, a dual specificity NUDT enzyme that attacks diadenosine polyphosphates and diphosphoinositol polyphosphates

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scholarly article

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Site-directed mutagenesis of diphosphoinositol polyphosphate phosphohydrolase, a dual specificity NUDT enzyme that attacks diadenosine polyphosphates and diphosphoinositol polyphosphates (English)

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Nudix hydrolase 3

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GOA release 2020-03-11

diphosphoinositol polyphosphate catabolic process

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GOA release 2020-03-11

author name string

X Yang

1

author given names

X

author last names

Yang

1 reference

PubMed publication ID

7 February 2023

S T Safrany

2

author given names

S T

author last names

Safrany

1 reference

PubMed publication ID

7 February 2023

S B Shears

3

author given names

S B

author last names

Shears

1 reference

PubMed publication ID

7 February 2023

language of work or name

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publication date

10 December 1999

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Journal of Biological Chemistry

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274

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50

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35434-40

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A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase

1 reference

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Synthesis and metabolism of bis-diphosphoinositol tetrakisphosphate in vitro and in vivo

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Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells

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The interaction of coatomer with inositol polyphosphates is conserved in Saccharomyces cerevisiae

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Accumulation of [3H]-inositol into inositol polyphosphates during development of Dictyostelium

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Inositol phosphates in barley (Hordeum vulgare L.) aleurone tissue are stereochemically similar to the products of breakdown of InsP6 in vitro by wheat-bran phytase

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Identification and purification of diphosphoinositol pentakisphosphate kinase, which synthesizes the inositol pyrophosphate bis(diphospho)inositol tetrakisphosphate

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Purified inositol hexakisphosphate kinase is an ATP synthase: diphosphoinositol pentakisphosphate as a high-energy phosphate donor

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A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export

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Turnover of inositol pentakisphosphates, inositol hexakisphosphate and diphosphoinositol polyphosphates in primary cultured hepatocytes

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Turnover of bis-diphosphoinositol tetrakisphosphate in a smooth muscle cell line is regulated by beta2-adrenergic receptors through a cAMP-mediated, A-kinase-independent mechanism

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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

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Diadenosine 5',5"-P1,P5-pentaphosphate harbors the properties of a signaling molecule in the heart.

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The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes

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Calculation of protein extinction coefficients from amino acid sequence data

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Schizosaccharomyces pombe Aps1, a diadenosine 5',5' "-P1, P6-hexaphosphate hydrolase that is a member of the nudix (MutT) family of hydrolases: cloning of the gene and characterization of the purified enzyme

1 reference

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Orf186 Represents a New Member of the Nudix Hydrolases, Active on Adenosine(5′)triphospho(5′)adenosine, ADP-ribose, and NADH

1 reference

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Significance of the conserved amino acid sequence for human MTH1 protein with antimutator activity

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The role of Glu 57 in the mechanism of the Escherichia coli MutT enzyme by mutagenesis and heteronuclear NMR.

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Solution structure of the quaternary MutT-M2+-AMPCPP-M2+ complex and mechanism of its pyrophosphohydrolase action

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A novel GDP-mannose mannosyl hydrolase shares homology with the MutT family of enzymes.

1 reference

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A highly conserved sequence motif defining the family of MutT-related proteins from eubacteria, eukaryotes and viruses

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Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases

1 reference

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The glycine-rich sequence of protein kinases: a multifunctional element

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The P-loop--a common motif in ATP- and GTP-binding proteins

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Active site comparisons highlight structural similarities between myosin and other P-loop proteins

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Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation

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The gene, ialA, associated with the invasion of human erythrocytes by Bartonella bacilliformis, designates a nudix hydrolase active on dinucleoside 5'-polyphosphates

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Diphospho-myo-inositol phosphates from Dictyostelium identified as D-6-diphospho-myo-inositol pentakisphosphate and D-5,6-bisdiphospho-myo-inositol tetrakisphosphate

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NMR Studies of the Conformations and Location of Nucleotides Bound to the Escherichia coli MutT Enzyme

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Diadenosine phosphates and the physiological control of blood pressure

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The IalA invasion gene of Bartonella bacilliformis encodes a (de)nucleoside polyphosphate hydrolase of the MutT motif family and has homologs in other invasive bacteria

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Diphospho-myo-inositol phosphates in Dictyostelium and Polysphondylium: identification of a new bisdiphospho-myo-inositol tetrakisphosphate

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Identifiers

10.1074/JBC.274.50.35434

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