The catalytic center of glucose-6-phosphatase. HIS176 is the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis (Q24300780)

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English	The catalytic center of glucose-6-phosphatase. HIS176 is the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis	scientific article

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scholarly article

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The catalytic center of glucose-6-phosphatase. HIS176 is the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis (English)

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Glucose-6-phosphatase catalytic subunit

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GOA release 2020-03-11

phosphate ion binding

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GOA release 2020-03-11

author name string

Abhijit Ghosh

1

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Jeng-Jer Shieh

2

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Chi-Jiunn Pan

3

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Mao-Sen Sun

4

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Janice Yang Chou

5

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language of work or name

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publication date

6 September 2002

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Journal of Biological Chemistry

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277

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36

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32837-42

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Identification of mutations in the glucose-6-phosphatase gene in Czech and Slovak patients with glycogen storage disease type ia, including novel mutations K76N, V166A and 540del5

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Identification of a novel phosphatase sequence motif

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Isolation of a cDNA for the catalytic subunit of rat liver glucose-6-phosphatase: regulation of gene expression in FAO hepatoma cells by insulin, dexamethasone and cAMP.

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Isolation and Nucleotide Sequence of Canine Glucose-6-phosphatase mRNA: Identification of Mutation in Puppies with Glycogen Storage Disease Type Ia

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Protein-bound phosphoryl histidine: a probable intermediate in the microsomal glucose-6-phosphatase-inorganic pyrophosphatase reaction.

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A new model for the membrane topology of glucose‐6‐phosphatase: the enzyme involved in von Gierke disease

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'In gel' cleavage with cyanogen bromide for protein internal sequencing

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Molecular Genetics of Type 1 Glycogen Storage Diseases

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Molecular aspects of glycogen storage disease type Ia in Turkish patients: a novel mutation in the glucose-6-phosphatase gene

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From phosphatases to vanadium peroxidases: a similar architecture of the active site

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Structure-function analysis of human glucose-6-phosphatase, the enzyme deficient in glycogen storage disease type 1a.

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Transmembrane topology of glucose-6-phosphatase

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Asparagine-linked oligosaccharides are localized to a luminal hydrophilic loop in human glucose-6-phosphatase

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Heterologous Expression of the Vanadium-containing Chloroperoxidase fromCurvularia inaequalisinSaccharomyces cerevisiaeand Site-directed Mutagenesis of the Active Site Residues His496, Lys353, Arg360, and Arg490

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Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase from the fungus Curvularia inaequalis. Implications for the catalytic mechanisms

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The molecular basis of glycogen storage disease type 1a: structure and function analysis of mutations in glucose-6-phosphatase

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Identification of Membrane-Bound Phosphoglucomutase and Glucose-6 Phosphatase by 32P-Labeling of Rat Liver Microsomal Membrane Proteins with 32P-Glucose-6 Phosphate1

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Mutations in the glucose-6-phosphatase gene that cause glycogen storage disease type 1a

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The molecular basis of type 1 glycogen storage diseases

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Identifiers

10.1074/JBC.M201853200

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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