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Information on EC 2.7.1.2 - glucokinase and Organism(s) Trypanosoma cruzi and UniProt Accession Q4E4E1

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IUBMB Comments
A group of enzymes found in invertebrates and microorganisms that are highly specific for glucose.
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This record set is specific for:
Trypanosoma cruzi
UNIPROT: Q4E4E1
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Word Map
The taxonomic range for the selected organisms is: Trypanosoma cruzi
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
glucokinase, atp-dependent glucokinase, tcglck, atp-glk, sgglka, tte0090, klglk1, sw2155, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glucokinase 1
-
glucokinase (phosphorylating)
-
-
-
-
kinase, gluco- (phosphorylating)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-glucose 6-phosphotransferase
A group of enzymes found in invertebrates and microorganisms that are highly specific for glucose.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-36-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-glucose
ADP + D-glucose 6-phosphate
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-deoxy-2-([[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]amino)-beta-D-glucopyranose
-
2-deoxy-2-[[3-(4-hydroxyphenyl)propanoyl]amino]-alpha-D-glucopyranose
186fold selectivity for Trypanosoma cruzi over human enzyme
2-[[(benzyloxy)carbonyl]amino]-2-deoxy-beta-D-glucopyranose
245fold selectivity for Trypanosoma cruzi over human enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.95 - 1
D-glucose
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.8 - 1492
D-glucose
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0041
2-deoxy-2-([[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]amino)-beta-D-glucopyranose
His-tagged recombinant protein, pH 7.2, 22°C
0.0013
2-deoxy-2-[[3-(4-hydroxyphenyl)propanoyl]amino]-alpha-D-glucopyranose
His-tagged recombinant protein, pH 7.2, 22°C
0.00071
2-[[(benzyloxy)carbonyl]amino]-2-deoxy-beta-D-glucopyranose
His-tagged recombinant protein, pH 7.2, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
x * 43000, the enzyme may occur as a monomer or dimer, dependent on the protein concentration, SDS-PAGE
46000
monomer, gel filtration
86000
dimer, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43000, the enzyme may occur as a monomer or dimer, dependent on the protein concentration, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures in complexes with inhibitors 2-[[(benzyloxy)carbonyl]amino]-2-deoxy-beta-D-glucopyranose, 2-deoxy-2-[[3-(4-hydroxyphenyl)propanoyl]amino]-alpha-D-glucopyranose, 2-deoxy-2-([[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]amino)-beta-D-glucopyranose. The analogues all share a common glucose moietythat preserves key enzyme-substrate hydrogen bonding interactions with the monosaccharide hydroxyl groups from C1, C3, C4,and C6. The C2 hydroxyl is replaced by a NH group and also par-ticipates in the key hydrogen bonding
crystals of TcGlcK in complex with D-glucose and ADP are obtained by the hanging-drop, vapor-diffusion method, using PEG3350 as precipitant agent and diammonium hydrogen citrate as additive. A complete native dataset is collected to 2.1 A maximum resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged recombinant TcGlcK is expressed in the Escherichia coli BL21 strain and purified to homogeneity by nickel affinity chromatography
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cordeiro, A.T.; Caceres, A.J.; Vertommen, D.; Concepcion, J.L.; Michels, P.A.; Versees, W.
The crystal structure of Trypanosoma cruzi glucokinase reveals features determining oligomerization and anomer specificity of hexose-phosphorylating enzymes
J. Mol. Biol.
372
1215-1226
2007
Trypanosoma cruzi (Q4E4E1), Trypanosoma cruzi
Manually annotated by BRENDA team
Caceres, A.J.; Quinones, W.; Gualdron, M.; Cordeiro, A.; Avilan, L.; Michels, P.A.; Concepcion, J.L.
Molecular and biochemical characterization of novel glucokinases from Trypanosoma cruzi and Leishmania spp
Mol. Biochem. Parasitol.
156
235-245
2007
Trypanosoma cruzi (Q4E4E1), Trypanosoma cruzi, Leishmania major (Q4Q1I9), Leishmania major
Manually annotated by BRENDA team
DAntonio, E.L.; Deinema, M.S.; Kearns, S.P.; Frey, T.A.; Tanghe, S.; Perry, K.; Roy, T.A.; Gracz, H.S.; Rodriguez, A.; DAntonio, J.
Structure-based approach to the identification of a novel group of selective glucosamine analogue inhibitors of Trypanosoma cruzi glucokinase
Mol. Biochem. Parasitol.
204
64-76
2015
Trypanosoma cruzi (Q4E4E1), Trypanosoma cruzi, Trypanosoma cruzi CL Brener (Q4E4E1)
Manually annotated by BRENDA team