2.7.1.147: ADP-specific glucose/glucosamine kinase
This is an abbreviated version!
For detailed information about ADP-specific glucose/glucosamine kinase, go to the full flat file.
Word Map on EC 2.7.1.147
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2.7.1.147
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hyperthermophilic
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thermococcus
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embden-meyerhof
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litoralis
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phosphofructokinases
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jannaschii
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furiosus
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glucokinases
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ribokinase
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methanococcales
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thermococcales
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6-phosphofructokinase
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hexokinases
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atp-pfks
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methanosarcinales
- 2.7.1.147
-
hyperthermophilic
- thermococcus
-
embden-meyerhof
- litoralis
-
phosphofructokinases
- jannaschii
- furiosus
- glucokinases
- ribokinase
- methanococcales
- thermococcales
- 6-phosphofructokinase
- hexokinases
- atp-pfks
- methanosarcinales
Reaction
Synonyms
ADP-dependent glucokinase, ADP-dependent hexokinase, ADP-dependent kinase, ADP-GK, ADP-HK, ADP-Pfk, ADP-specific glucokinase, ADP:D-glucose 6-phosphotransferase, ADPGK, ancGK/PFK, AncMsPFK/GK, bifunctional ADP-dependent phosphofructokinase/glucokinase, GlcN kinase, glucosamine kinase, MevePFK/GK, MjPFK/GK, MmazPFK/GK, MmPFK/GK, More, NagC4, pfGK, pfkC, PhPFK, TK1110, tlGK
ECTree
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General Information
General Information on EC 2.7.1.147 - ADP-specific glucose/glucosamine kinase
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evolution
malfunction
metabolism
physiological function
additional information
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consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
evolution
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
evolution
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
evolution
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
evolution
kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons
evolution
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
evolution
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei posseses a bifunctional MmazPFK/GK
evolution
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the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei posseses a bifunctional MmazPFK/GK
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evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei posseses a bifunctional MmazPFK/GK
-
evolution
-
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei posseses a bifunctional MmazPFK/GK
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei posseses a bifunctional MmazPFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei posseses a bifunctional MmazPFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
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down-regulation of ADPGK or GPD2 abundance inhibits oxidative signal generation and induction of NF-kappaB-dependent gene expression, whereas over-expression of ADPGK potentiates them
malfunction
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overexpression or suppression of ADPGK does not show any relevant effect
malfunction
ADPGK knock-out Ramos BL cells display abated in vitro and in vivo tumour aggressiveness, via tumour-macrophage co-culture, migration and Zebrafish xenograft studies. Perturbed glycolysis and visibly reduced markers of Warburg effect in ADPGK knock-out cells, finally leading to apoptosis. Knock-out cells show repression of MYC proto-oncogene, and up to four-fold reduction in accumulated mutations in translocated MYC
malfunction
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ADPGK knockdown in zebrafish embryos leads to short, dorsalized body axis induced by elevated apoptosis. ADPGK hypomorphic zebrafish display dysfunctional glucose metabolism
malfunction
TK1110 disruption results in almost complete impairment in chitin degradation, and a complete loss of chitin-dependent H2 production
malfunction
upon activation, ADPGK knockout Jurkat T cells display increased cell death and ER stress. The increase in cell death results from a metabolic catastrophe and knockout cells displayed severely disturbed energy metabolism hindering induction of Warburg phenotype
malfunction
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TK1110 disruption results in almost complete impairment in chitin degradation, and a complete loss of chitin-dependent H2 production
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human ADPGK catalyses ADP-dependent phosphorylation of glucose in vitro
metabolism
enzyme TK1110 functions as the glucosamine kinase responsible for the chitin degradation in Thermococcus kodakarensis
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T cell activation-induced mitochondrial ROS production and NF-kappaB-driven gene expression depend on activation of ADPGK. ADPGK activation is accompanied by a rapid glucose uptake, downregulation of mitochondrial oxygen consumption, and deviation of glycolysis toward the glycerol-3-phosphate dehydrogenase shuttle
physiological function
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the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
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knockout of inc finger nucleases in each H-460 and HCT-11 cells lead to frameshift mutations in all alleles at the target site in exon 1 of ADP-dependent glucokinase ADPGK, and are ADPGK-null by immunoblotting. ADPGK knockout has little or noeffect on cell proliferation, but compromises the ability of H-460 cells to survive siRNA silencing of hexokinase-2 under oxic conditions and anoxia. No such changes are found when ADPGK is knocked out in HCT-116 cells. Knockout of ADPGK in HCT-116 cells causes few changes in global gene expression, while knockout of ADPGK in H-460 cells causes notable up-regulation of mRNAs encoding cell adhesion proteins. No consistent effect on glycolysis under oxic conditions in a variety of media is observed. Oxygen consumption rates are generally lower in the ADPGK knockouts
physiological function
the enzyme functions as the glucosamine kinase responsible for the chitin degradation
physiological function
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the enzyme plays a critical role in T cell receptor activation-induced remodeling of energy metabolism. The enzyme is part of a glucose sensing system in the ER modulating metabolism via regulation of N- and O-glycosylation
physiological function
the enzyme plays a critical role in T cell receptor activation-induced remodeling of energy metabolism. The enzyme is part of a glucose sensing system in the ER modulating metabolism via regulation of N- and O-glycosylation
physiological function
the enzyme plays a major role in T-cell activation and induction of Warburg effect
physiological function
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the enzyme functions as the glucosamine kinase responsible for the chitin degradation
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enzyme structure and homology modeling
additional information
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
additional information
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enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
additional information
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molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
additional information
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
additional information
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
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additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
-
additional information
-
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
-
additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
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additional information
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enzyme structure and homology modeling
-
additional information
-
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
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