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The three dimensional structure of sheep liver 6-phosphogluconate dehydrogenase at 2.6 A resolution.
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Binding of coenzyme and substrate and coenzyme analogues to 6-phosphogluconate dehydrogenase from sheep liver. An X-ray study at 0.6 nm resolution.
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A 2.8 A resolution structure of 6-phosphogluconate dehydrogenase from the protozoan parasite Trypanosoma brucei: comparison with the sheep enzyme accounts for differences in activity with coenzyme and substrate analogues.
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Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism.
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Is there an alternating site co-operativity between the two subunits of lamb liver 6-phosphogluconate dehydrogenase?
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Kinetic studies of 6-phosphogluconate dehydrogenase from sheep liver.
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Fluorescein 5'-isothiocyanate binds to the coenzyme and not to the substrate binding site of lamb liver 6-phosphogluconate dehydrogenase.
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Importance in catalysis of the 6-phosphate-binding site of 6-phosphogluconate in sheep liver 6-phosphogluconate dehydrogenase.
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Role of the S128, H186, and N187 triad in substrate binding and decarboxylation in the sheep liver 6-phosphogluconate dehydrogenase reaction.
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Chemical modification of sheep-liver 6-phosphogluconate dehydrogenase by diethylpyrocarbonate. Evidence for an essential histidine residue.
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6-Phosphogluconate dehydrogenase and its crystal structures.
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An Integrated Biochemical, Proteomics, and Metabolomics Approach for Supporting Medicinal Value of Panax ginseng Fruits.
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Sorting the chaff from the wheat at the PDB.
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Identification of a cDNA encoding 6-phosphogluconate dehydrogenase from a human heart cDNA library.
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NAD(+)-dependent formate dehydrogenase.
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The NADPH binding site on beef liver catalase.
Proc Natl Acad Sci U S A. 1985 Mar;82(6):1604-8. doi: 10.1073/pnas.82.6.1604.
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The chemical mechanism of sheep liver 6-phosphogluconate dehydrogenase. A Schiff-base intermediate is not involved.
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Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.
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Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase.
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1
Amino acid sequence around the pyridoxal 5'-phosphate binding sites of 6-phosphogluconate dehydrogenase.
Biochim Biophys Acta. 1981 Jan 15;657(1):232-42. doi: 10.1016/0005-2744(81)90147-9.
2
Evidence for multiple pairs of vicinal thiols in some proteins.
J Biol Chem. 1981 Jan 10;256(1):451-5.
3
Substrate-induced intramolecular proton transfer in 6-phosphogluconate dehydrogenase from Candida utilis.
Biochim Biophys Acta. 1981 Nov 13;662(1):163-4. doi: 10.1016/0005-2744(81)90238-2.
4
Pyridoxal 5'-phosphate as a specific photosensitizer for histidine residue at the active site of 6-phosphogluconate dehydrogenase.
Arch Biochem Biophys. 1969 Aug;133(1):112-8. doi: 10.1016/0003-9861(69)90494-9.
5
Evidence of a critical histidine residue in 6-phosphogluconate dehydrogenase from Candida utilis.
Biochemistry. 1968 Apr;7(4):1514-8. doi: 10.1021/bi00844a038.
6
Crystalline 6-phosphogluconate dehydrogenase from sheep liver.
Eur J Biochem. 1973 Oct 5;38(2):229-38. doi: 10.1111/j.1432-1033.1973.tb03054.x.
7
Sheep liver 6-phosphogluconate dehydrogenase: isolation procedure and effect of pH, ionic strength, and metal ions on the kinetic parameters.
Arch Biochem Biophys. 1973 Feb;154(2):623-35. doi: 10.1016/0003-9861(73)90017-9.
8
Studies of 6-phosphogluconate dehydrogenase from sheep liver. 2. Kinetics of the oxidative-decarboxylation reaction, coenzyme binding and analyses for metals.
Eur J Biochem. 1972 May 23;27(2):251-8. doi: 10.1111/j.1432-1033.1972.tb01834.x.
9
Evidences for the involvement of a histidine residue in the binding of the substrate to the 6-phosphogluconate dehydrogenase.
Arch Biochem Biophys. 1972 Jun;150(2):503-10. doi: 10.1016/0003-9861(72)90068-9.
10
Evidence for a tyrosine residue at the triphosphopyridine nucleotide-binding site of 6-phosphogluconate dehydrogenase.
Arch Biochem Biophys. 1971 Dec;147(2):487-92. doi: 10.1016/0003-9861(71)90405-x.
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