2.7.2.3: phosphoglycerate kinase
This is an abbreviated version!
For detailed information about phosphoglycerate kinase, go to the full flat file.
Word Map on EC 2.7.2.3
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2.7.2.3
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glyceraldehyde-3-phosphate
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x-linked
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aldolase
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enolase
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x-chromosome
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hexokinase
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erythrocyte
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phosphofructokinase
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glucose-6-phosphate
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gapdh
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marrow
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lentiviral
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anemia
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trypanosoma
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hypoxanthine
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triosephosphate
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hematopoietic
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mutase
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glyceraldehyde
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brucei
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hypoxia-inducible
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hemolytic
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phosphoribosyltransferase
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cytomegalovirus
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glycosomal
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triose
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x-chromosome-linked
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tpi
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x-inactivation
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methylation-sensitive
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myoglobinuria
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n-domain
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genorm
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calvin
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hif-1alpha
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hpaii
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mgadp
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fructose-1,6-bisphosphate
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fructose-bisphosphate
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2,3-diphosphoglycerate
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myeloproliferative
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self-inactivating
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phosphoglucose
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microbody
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ligation-mediated
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atp-generating
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glucosephosphate
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alpha-enolase
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medicine
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phosphoribulokinase
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allozyme
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analysis
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biofuel production
- 2.7.2.3
- glyceraldehyde-3-phosphate
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x-linked
- aldolase
- enolase
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x-chromosome
- hexokinase
- erythrocyte
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phosphofructokinase
- glucose-6-phosphate
- gapdh
- marrow
-
lentiviral
- anemia
- trypanosoma
- hypoxanthine
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triosephosphate
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hematopoietic
- mutase
- glyceraldehyde
- brucei
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hypoxia-inducible
-
hemolytic
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phosphoribosyltransferase
- cytomegalovirus
- glycosomal
- triose
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x-chromosome-linked
- tpi
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x-inactivation
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methylation-sensitive
- myoglobinuria
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n-domain
-
genorm
-
calvin
- hif-1alpha
- hpaii
- mgadp
- fructose-1,6-bisphosphate
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fructose-bisphosphate
- 2,3-diphosphoglycerate
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myeloproliferative
-
self-inactivating
-
phosphoglucose
- microbody
-
ligation-mediated
-
atp-generating
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glucosephosphate
- alpha-enolase
- medicine
- phosphoribulokinase
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allozyme
- analysis
- biofuel production
Reaction
Synonyms
3-PGK, 3-phosphoglycerate 1-phosphotransferase, 3-phosphoglycerate kinase, 3-phosphoglycerate phosphokinase, 3-phosphoglyceric acid kinase, 3-phosphoglyceric acid phosphokinase, 3-phosphoglyceric kinase, AbPGK, ATP-3-phospho-D-glycerate-1-phosphotransferase, ATP:3-phospho-D-glycerate 1-phosphotransferase, ATP:D-3-phosphoglycerate 1-phosphotransferase, chl-PGK, glycerate 3-phosphate kinase, glycerophosphate kinase, HacPGK1, HacPGK2, HapPGK, hPGK, HsPGK, human 3-phosphoglycerate kinase, kinase (phosphorylating), phosphoglycerate, Mfer_0156, OsPGK2, P-glycerate kinase, PAS-PGK, PfPGK, PGK, PGK 1, PGK-1, PGK-2, pgk-B, PGK1, PGK2, Pgk3, Pgk5, PGKA, PGKase-1, PGKB, PGKC, pgkp1, pgkp2, phosphoglycerate kinase, phosphoglycerate kinase 1, phosphoglycerate kinase 2, phosphoglycerate kinase B, phosphoglycerate kinase-1, phosphoglyceric acid kinase, phosphoglyceric kinase, phosphoglycerokinase, PwPGK, SjPGK, SSO0527, testis-specific phosphoglycerate kinase 2, TRSC58_02767, X chromosome-linked phosphoglycerate kinase-1
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
biofuel production
proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol
medicine
additional information
analysis
computational docking method for analysis of the docking of both aromatic and aliphatic bisphosphonates to the Trypanosoma brucei PGK
analysis
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first quantitative analysis of the binding of alkyl bisphosphonates to yeast PGK, with activities being predicted within, on average, a factor of 4 over a 2500x overall range in activity
analysis
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first quantitative analysis of the inhibition of human phosphoglycerate kinase by aromatic bisphosphonates by 3D-QSAR (CoMFA, CoMSIA) and pharmacophore modeling methods
analysis
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development of a sensitive sandwich ELISA using an immuno-affinity-purified chicken polyclonal antibody for capturing PGK1 and an immuno-affinity-purified rabbit polyclonal antibody for detecting it. The sandwich ELISA can be used to quantify PGK1 levels in conditioned media of cell cultures for in vitro PGK1 export studies and in human serum for potential use ascreen for cancer
analysis
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PGK1 might be a potential protein biomarker of intracellular oxidative status
analysis
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in situ PCR is useful for detecting PGK-1 gene in paraffin-embedded sections under optimized conditions of both PCR cycle number and proteinase K concentration
medicine
enzyme of parasite is target for vaccine and drug development, enzyme elicits antibodies and can therefore be utilized as immunoreagent in serodiagnostics for clonorchiasis
medicine
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inhibition of the enzyme can provide a method of treatment for cardiovascular and respiratory disorders, construction of possible specific fluoro-phosphonate inhibitors
medicine
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overexpression or down-regulation of PGK affects the cytotoxicity of beta-L-dioxolane-cytidine, which is under clinical trials for treating cancer, but not that of beta-D-2',2'-difluorodeoxycytidine under normoxic conditions, overexpression of PGK does not further increase the cytotoxicity of beta-L-dioxolane-cytidine under hypoxic conditions
medicine
PGK deficiency (D164V mutation) is a rare X-linked disease that is characterised by mild to severe haemolytic anaemia, rhabdomyolysis, and variable defects in the central nervous system, it is a recurrent mutation
medicine
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PGK1 is a potential biomarker and/or therapeutic target for pancreatic ductal adenocarcinoma
medicine
two missense mutations in patients of Spanish origin with a severe life-long chronic haemolytic anaemia associated with progressive neurological impairment. One patient with an amino acid change of Ile to Asn at 46th position from the NH2-terminal serine residue, the second patient with a Ser319Asn amino acid substitution. In both cases, the mutations do not modify any of the PGK binding sites for ATP or 3-phospho-D-glycerate, so their consequence is related to a loss of enzyme stability rather than a decrease of enzyme catalytic function
medicine
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PGK-1 may be an important therapeutic target for pharmacological or gene therapy intervention in non-small cell lung carcinoma
medicine
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the gene encoding the erythrocyte enzyme PGK1, is X-linked. Mutations of this gene may cause chronic haemolysis with or without mental retardation and they may cause myopathies, often with episodes of myoglobinuria, or a combination of these clinical manifestations
medicine
the X-linked recessive disease phosphoglycerate kinase deficiency is caused by altered expression of the PGK1 enzyme, which causes muscle stiffness, hemolytic anemia, and mental retardation. The PGK1 gene is charaterized in a family of two brothers, two sisters, and their parents. A single mutation in exon 6, which is associated with the pattern of inheritance of PGK1 deficiency, is observed. This silent G213G mutation is localized to the conserved exon-intron boundary. A method for quantification of PGK1 mRNA is developed. A marked reduction in PGK1 mRNA is demonstrated in both brothers with the disease. A smaller decrease in PGK1 expression is observed in one sister with symptoms of PGK deficiency and in her mother. Only the normal PGK1 allele is expressed in the two heterozygous women. Whereas most known PGK1 mutations cause amino acid alterations, this study indicates that inhibition of the transcription mechanism is the cause of PGK deficiency
medicine
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PGK1 may serve as prognostic marker and/or be a potential therapeutic target to prevent dissemination of gastric carcinoma cells into the peritoneum
medicine
transgenic mice ubiquitously expressing enhanced green fluorescent protein (EGFP) under the control of the phosphoglycerate kinase 1 promoter by allotransplantation of transgenic mice ovaries may be useful for studies assessing the use of gene therapy of bone marrow or nerve cells, as well as for tumorigenesis and organ transplantation studies
additional information
Arg148 as a key residue involved in open-to-closed transition, during catalysis, a conformational change occurs that brings the N- and C-domains of PGK closer together
additional information
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Arg148 as a key residue involved in open-to-closed transition, during catalysis, a conformational change occurs that brings the N- and C-domains of PGK closer together
additional information
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formation of a double-sided H-bond network, which affects substantially the shape of the main molecular hinge at beta-strand L, under the concerted action of both substrates
additional information
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hierarchic finite level landscape model that quantitatively describes the refolding of yeast phosphoglycerate kinase from 1 ms to 15 min. Early steps of the folding process happen in the upper region of the landscape, where the surface has a hierarchic structure. This leads to stretched kinetics in the early phase of the folding. The lower region of the energy landscape is dominated by a trap that reflects the accumulation of molten globule intermediate state. From this intermediate, the protein can reach the global energy minimum corresponding to the native state through a cross-barrier folding step
additional information
immobilizing PGK on solid supports like glass or muscovite mica does not strongly modify its enzymatic activity, guideline for biosensors made with the method of Tapping Mode atomic force microscopy whenever a rapid assessment of the remaining surface activity is needed
additional information
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immobilizing PGK on solid supports like glass or muscovite mica does not strongly modify its enzymatic activity, guideline for biosensors made with the method of Tapping Mode atomic force microscopy whenever a rapid assessment of the remaining surface activity is needed
additional information
importance of interdomain contacts in the overall dynamics of the protein, hinge bending in the nanosecond timescale, the two domains of the complete enzyme exhibit rigid body motions anticorrelated with respect to each other. The correlation of the intradomain motions of both domains converges, yielding a distinct correlation map in the enzyme. In the isolated domain simulations, in which interdomain interactions cannot occur, the correlation of domain motions no longer converges and shows a very small correlation during the same simulation time
additional information
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importance of interdomain contacts in the overall dynamics of the protein, hinge bending in the nanosecond timescale, the two domains of the complete enzyme exhibit rigid body motions anticorrelated with respect to each other. The correlation of the intradomain motions of both domains converges, yielding a distinct correlation map in the enzyme. In the isolated domain simulations, in which interdomain interactions cannot occur, the correlation of domain motions no longer converges and shows a very small correlation during the same simulation time
additional information
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interacts specifically with the 3'-UTR of Bamboo mosaic virus RNA, associates with the poly(A) tail
additional information
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not resistant to proteolytic cleavage, both domains of the yeast protein fold in isolation into stable structures, extremely similar tertiary structures and global stabilities as compared to the homologous Escherichia coli PGK, but significant differences in proteolysis
additional information
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PGKB mRNA and PGKB protein are much more abundant in the procyclic life-cycle stage than in bloodstream forms, whereas PGKC mRNA and PGKC protein are specific to bloodstream forms. PGKC 3'-UTR exerts strong regulatory effects, they are exerted at the levels of both mRNA stability and translation. PGKC3'-UTR contains some elements which promote active degradation in procyclic forms, but it also is responsible for an active stabilisation process in bloodstream forms
additional information
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polypyrimidine tract binding protein 2 is a trans-acting factor that helps to stabilize PGK2 mRNA in male mouse germ cells, specifically binds to the F1 region of the PGK2 3'-UTR
additional information
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resistant to proteolytic cleavage, the C-domain of PGK cannot be expressed or fold independently of the N-domain, extremely similar tertiary structures and global stabilities as compared to the homologous Saccharomyces cerevisiae PGK, but significant differences in proteolysis
additional information
resistant to proteolytic cleavage, the C-domain of PGK cannot be expressed or fold independently of the N-domain, extremely similar tertiary structures and global stabilities as compared to the homologous Saccharomyces cerevisiae PGK, but significant differences in proteolysis
additional information
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submolecular mechanism of amyloid formation based on a model system of PGK, evaluated by microscopic measurements and tryptophan fluorescence. Interactions between the polypeptide chains of the two domains of the protein direct the misfolding process from the early steps to the amyloid formation, and influence the final structure. Kinetics of misfolding is different for the individual domains. Misfolding of the domains within the complete protein is synchronized indicating that domain-domain interactions direct the misfolding and amyloid formation mechanism
