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Information on EC 3.1.1.31 - 6-phosphogluconolactonase and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.31 6-phosphogluconolactonase
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This record set is specific for:
Homo sapiens
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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-phosphoglucono-gamma-lactonase, xoo2316, og1rf_11582, 6-phosphogluconolactonase 3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-PGL
-
-
-
-
6-phospho-D-glucose-delta-lactone hydrolase
-
-
-
-
6-phosphoglucono-gamma-lactonase
-
-
-
-
6-phosphogluconolactonase
lactonase, phosphoglucono-
-
-
-
-
PGL
-
-
-
-
phosphogluconolactonase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
show the reaction diagram
first order reaction
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
6-phospho-D-glucono-1,5-lactone lactonohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37278-45-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-phospho-D-glucono-1,4-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
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
-
-
?
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
6-phospho-D-glucono-1,5-lactone + H2O
6-phospho-D-gluconate
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
-
0.06 M, 55% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1065
recombinant h6PGL, substrate is 6-phospho-D-glucono-1,5-lactone, pH 7.0, 25°C
3330
recombinant 6PGL
54.2
-
recombinant 6PGL
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
G6PE_HUMAN
791
0
88893
Swiss-Prot
Secretory Pathway (Reliability: 1)
6PGL_HUMAN
258
0
27547
Swiss-Prot
other Location (Reliability: 4)
A0A0K0K1K7_HUMAN
258
0
27547
TrEMBL
other Location (Reliability: 4)
M0R261_HUMAN
216
0
22997
TrEMBL
other Location (Reliability: 4)
M0R1L2_HUMAN
147
0
16365
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27529
-
1 * 27529, calculation from sequence of amino acids
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 27529, calculation from sequence of amino acids
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
22°C, enzyme activity in erythrocytes is stable for 6 days stored in citrate dextrose, heparin and EDTA as anticoagulants
-
4°C, enzyme activity in erythrocytes is stable for 20 days stored in citrate dextrose, heparin and EDTA as anticoagulants
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant 6PGL
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene h6PGL, overexpression as N-terminally His-tagged enzyme in Escherichia coli strain BL21 using vector pRAREII
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bauer, H.P.; Srihari, T.; Jochims, J.C.; Hofer, H.W.
6-Phosphogluconolactonase. Purification, properties and activities in various tissues
Eur. J. Biochem.
133
163-168
1983
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Beutler, E.; Kuhl, W.; Gelbart, T.
Blood cell phosphogluconolactonase: assay and properties
Br. J. Haematol.
62
577-586
1986
Homo sapiens
Manually annotated by BRENDA team
Rakitzis, E.T.; Papandreou, P.
Kinetic analysis of 6-phosphogluconolactone hydrolysis in hemolysates
Biochem. Mol. Biol. Int.
37
747-755
1995
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team