Enzyme

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     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.9
Description:Glucose-6-phosphatase.
Cath: 1.10.150.240; 3.10.580.10; 3.40.1390.20; 3.90.1640.10; 3.90.80.10; 3.40.50.1000; 3.10.310.20;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.9
BRENDA Enzyme Link: BRENDA 3.1.3.9
KEGG Enzyme Link: KEGG3.1.3.9
BioCyc Enzyme Link: BioCyc 3.1.3.9
ExPASy Enzyme Link: ExPASy3.1.3.9
EC2PDB Enzyme Link: EC2PDB 3.1.3.9
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.9
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.9
IntEnz Enzyme Link: IntEnz 3.1.3.9
MEDLINE Enzyme Link: MEDLINE 3.1.3.9
MSA:

3.1.3.9;

Phylogenetic Tree:

3.1.3.9;

Uniprot:
M-CSA:
RHEA:44904 alpha-D-glucose 6-phosphate + H2O = alpha-D-glucose + phosphate
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

RHEA:16689 D-glucose 6-phosphate + H2O = D-glucose + phosphate
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Characterization of a membrane-regulated sugar phosphate phosphohydrolase from Lactobacillus casei.London J, Hausman SZ, Thompson J1985 Sep2993253
Purification of cerebral glucose-6-phosphatase. An enzyme involved in sleep.Anchors JM, Karnovsky ML1975 Aug 25169241
Enzymatic characterization of the pancreatic islet-specific glucose-6-phosphatase-related protein (IGRP).Petrolonis AJ, Yang Q, Tummino PJ, Fish SM, Prack AE, Jain S, Parsons TF, Li P, Dales NA, Ge L, Langston SP, Schuller AG, An WF, Tartaglia LA, Chen H, Hong SB2004 Apr 214722102
Identification and characterisation of a new human glucose-6-phosphatase isoform.Guionie O, Clottes E, Stafford K, Burchell A2003 Sep 1112965222