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EC Tree
The taxonomic range for the selected organisms is: Homo sapiens The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
6-phosphogluconolactonase, 6pgl, phosphogluconolactonase, glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase, g6pd-6pgl, 6-pgl, 6-phosphogluconolactonase 3, 6-phosphoglucono-gamma-lactonase, xoo2316, og1rf_11582,
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6-phosphogluconolactonase
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6-phospho-D-glucose-delta-lactone hydrolase
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6-phosphoglucono-gamma-lactonase
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6-phosphogluconolactonase
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lactonase, phosphoglucono-
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phosphogluconolactonase
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6PGL
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6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
first order reaction
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hydrolysis of carboxylic ester
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6-phospho-D-glucono-1,5-lactone lactonohydrolase
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6-phospho-D-glucono-1,4-lactone + H2O
6-phospho-D-gluconate
the gamma-lactone is more stable than the natural delta-lactone substrate. It contains a five-membered heterocyclic ring, whereas the delta-lactone contains a six-membered heterocyclic ring
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6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
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6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
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6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
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6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
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6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
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6-phosphogluconolactone
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6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
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6-phosphogluconolactone
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6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
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enzyme hydrolyzes both, the delta- and - gamma forms of 6-phosphogluconolactone
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6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
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6-phospho-D-gluconate
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6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
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second step in pentose phosphate pathway
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6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
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second step in pentose phosphate pathway
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6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
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6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
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(NH4)2SO4
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0.06 M, 55% inhibition
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6-phosphogluconolactonase deficiency
6-Phosphogluconolactonase deficiency, a hereditary erythrocyte enzyme deficiency: possible interaction with glucose-6-phosphate dehydrogenase deficiency.
Anemia, Hemolytic
6-Phosphogluconolactonase deficiency, a hereditary erythrocyte enzyme deficiency: possible interaction with glucose-6-phosphate dehydrogenase deficiency.
Brain Neoplasms
Imaging 6-Phosphogluconolactonase Activity in Brain Tumors In Vivo Using Hyperpolarized ?-[1-13C]gluconolactone.
Breast Neoplasms
Expression of Pentose Phosphate Pathway-Related Proteins in Breast Cancer.
Breast Neoplasms
Molecular-assisted immunohistochemical optimization.
glucose-6-phosphate dehydrogenase (nadp+) deficiency
6-Phosphogluconolactonase deficiency, a hereditary erythrocyte enzyme deficiency: possible interaction with glucose-6-phosphate dehydrogenase deficiency.
Glucosephosphate Dehydrogenase Deficiency
6-Phosphogluconolactonase deficiency, a hereditary erythrocyte enzyme deficiency: possible interaction with glucose-6-phosphate dehydrogenase deficiency.
Glucosephosphate Dehydrogenase Deficiency
Computer simulation of the metabolic consequences of the combined deficiency of 6-phosphogluconolactonase and glucose-6-phosphate dehydrogenase in human erythrocytes.
Malaria
Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase. A novel bifunctional enzyme in malaria parasites.
Neoplasm Metastasis
Differential Site-Based Expression of Pentose Phosphate Pathway-Related Proteins among Breast Cancer Metastases.
Neoplasms
Expression of Pentose Phosphate Pathway-Related Proteins in Breast Cancer.
Neoplasms
Imaging 6-Phosphogluconolactonase Activity in Brain Tumors In Vivo Using Hyperpolarized ?-[1-13C]gluconolactone.
Neoplasms
Novel breast cancer biomarkers identified by integrative proteomic and gene expression mapping.
Pancreatic Neoplasms
Proteomics finding heat shock protein 27 as a biomarker for resistance of pancreatic cancer cells to gemcitabine.
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additional information
additional information
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additional information
additional information
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additional information
additional information
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1065
recombinant h6PGL, substrate is 6-phospho-D-glucono-1,5-lactone, pH 7.0, 25°C
additional information
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additional information
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additional information
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enzyme activity in lymphocytes, monocytes, granulocytes and platelets is 10 times as high as that in erythrocytes, activity is independent of red cell age
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25
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25
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pH 7.0 provides favourable conditions for the enzyme assay
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SwissProt
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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6PGL_HUMAN
258
0
27547
Swiss-Prot
other Location (Reliability: 4 )
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27529
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1 * 27529, calculation from sequence of amino acids
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monomer
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1 * 27529, calculation from sequence of amino acids
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22°C, enzyme activity in erythrocytes is stable for 6 days stored in citrate dextrose, heparin and EDTA as anticoagulants
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4°C, enzyme activity in erythrocytes is stable for 20 days stored in citrate dextrose, heparin and EDTA as anticoagulants
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expression in Escherichia coli
gene h6PGL, overexpression as N-terminally His-tagged enzyme in Escherichia coli strain BL21 using vector pRAREII
expression in Escherichia coli
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Bauer, H.P.; Srihari, T.; Jochims, J.C.; Hofer, H.W.
6-Phosphogluconolactonase. Purification, properties and activities in various tissues
Eur. J. Biochem.
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163-168
1983
Bos taurus, Homo sapiens, Rattus norvegicus
brenda
Beutler, E.; Kuhl, W.; Gelbart, T.
Blood cell phosphogluconolactonase: assay and properties
Br. J. Haematol.
62
577-586
1986
Homo sapiens
brenda
Rakitzis, E.T.; Papandreou, P.
Kinetic analysis of 6-phosphogluconolactone hydrolysis in hemolysates
Biochem. Mol. Biol. Int.
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747-755
1995
Homo sapiens
brenda
Collard, F.; Collet, J.F.; Gerin, I.; Veiga-da-Cunha, M.; van Schaftingen, E.
Identification of the cDNA encoding human 6-phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway(1)
FEBS Lett.
459
223-226
1999
Homo sapiens
brenda
Clarke, J.L.; Scopes, D.A.; Sodeinde, O.; Mason, P.J.
Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase. A novel bifunctional enzyme in malaria parasites
Eur. J. Biochem.
268
2013-2019
2001
Homo sapiens, Plasmodium berghei
brenda
Miclet, E.; Stoven, V.; Michels, P.A.M.; Opperdoes, F.R.; Lallemand, J.Y.; Duffieux, F.
NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase
J. Biol. Chem.
276
34840-34846
2001
Homo sapiens (O95336), Homo sapiens, Plasmodium falciparum (Q27741), Plasmodium falciparum, Trypanosoma brucei (Q9GRG6), Trypanosoma brucei
brenda
Jortzik, E.; Mailu, B.M.; Preuss, J.; Fischer, M.; Bode, L.; Rahlfs, S.; Becker, K.
Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: a unique bifunctional enzyme from Plasmodium falciparum
Biochem. J.
436
641-650
2011
Plasmodium falciparum, Homo sapiens (O95336), Homo sapiens
brenda