Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency (Q27622024)

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English	Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency	scientific article

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scholarly article

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Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency (English)

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crystal structure

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Glucose-6-phosphate dehydrogenase

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author name string

S W Au

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S Gover

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V M Lam

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M J Adams

4

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language of work or name

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publication date

15 March 2000

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8

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3

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293-303

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Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress

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Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery

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Isolation of human glucose-6-phosphate dehydrogenase (G6PD) cDNA clones: primary structure of the protein and unusual 5' non-coding region

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Metabolism of human erythrocyte glucose-6-phosphate dehydrogenase. VI. Interconversion of multiple molecular forms.

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Genetic variants of human erythrocyte glucose-6-phosphate dehydrogenase. Discrete conformational states stabilized by NADP + and NADPH

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Amino acid substitutions at the dimer interface of human glucose-6-phosphate dehydrogenase that increase thermostability and reduce the stabilising effect of NADP

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Human erythrocyte glucose 6-phosphate dehydrogenase: electron microscope studies on structure and interconversion of tetramers, dimers and monomers

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Solution of the structure of tetrameric human glucose 6-phosphate dehydrogenase by molecular replacement

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Sequence identity between a lysine-containing peptide from Leuconostoc mesenteroides glucose-6-phosphate dehydrogenase and an active site peptide from human erythrocyte glucose-6-phosphate dehydrogenase

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Human erythrocyte glucose-6-phosphate dehydrogenase. Identification of a reactive lysyl residue labelled with pyridoxal 5'-phosphate

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Human glucose-6-phosphate dehydrogenase. Lysine 205 is dispensable for substrate binding but essential for catalysis.

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Lysine‐21 of Leuconostoc mesenteroides glucose 6‐phosphate dehydrogenase participates in substrate binding through charge–charge interaction

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Identification of an arginine residue in the dual coenzyme-specific glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides that plays a key role in binding NADP+ but not NAD+

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On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase

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10.1016/S0969-2126(00)00104-0

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Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

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PubMed publication ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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