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ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
2'-deoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2'-deoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
isozyme PGK1
-
-
?
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
beta-L(-)-dioxolanecytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L(-)-dioxolanecytidine 5'-diphosphate + 1,3-diphosphoglycerate
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-diphosphate + 1,3-diphosphoglycerate
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
-
-
-
-
?
dITP + 3-phospho-D-glycerate
dIDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
additional information
?
-
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
isozyme PGK1
-
-
?
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
3.6fold higher activity compared to 2'-deoxycytidine
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
infrared studies reveal unique vibrations associated with the phosphoglycerate kinase-ATP-3-phosphoglycerate ternary complex
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
the enzyme favors the forward reaction
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
the isolated N-terminal domain is soluble, monomeric, compactly folded, native-like in structure, and capable of binding 3-phospho-D-glycerate with high affinity
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
beta-L(-)-dioxolanecytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L(-)-dioxolanecytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
isozyme PGK1
-
-
?
beta-L(-)-dioxolanecytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L(-)-dioxolanecytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
3fold higher activity compared to 2'-deoxycytidine
-
-
?
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
isozyme PGK1
-
-
?
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
4fold higher activity compared to 2'-deoxycytidine
-
-
?
additional information
?
-
-
no activity with dCTP, dUTP, dTTP
-
-
?
additional information
?
-
-
2',3'-dideoxycytidine is a very poor substrate
-
-
?
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
-
enzyme is identical with the socalled host factor, which activates RNA transcription in Sendai virus, when bound in a complex with host tubulin and a complementary factor
-
-
?
additional information
?
-
-
pressure-jump unfolding kinetics of phosphoglycerate kinase at pressures between 50 and 150 MPa and time dependence of the conformational state of the protein followed by tryptophan fluorescence measurements from 30 s to 2 h: the activation volumes of the unfolding reaction are negative for the folded-intermediate, intermediate-unfolded, and unfolded-intermediate transitions
-
-
?
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Janson, C.A.; Cleland, W.W.
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
J. Biol. Chem.
249
2567-2571
1974
Saccharomyces cerevisiae
brenda
Watson, H.C.; Bryant, T.N.; Walker, N.P.C.; Shaw, P.J.; Wendell, P.L.
The active site of yeast phosphoglycerate kinase
Biochem. Soc. Trans.
5
652-654
1977
Saccharomyces cerevisiae, Equus caballus
brenda
Li, Y.K.; Byers, L.D.
Phosphonate inhibitors of glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase
Biochim. Biophys. Acta
1164
17-21
1993
Saccharomyces cerevisiae
brenda
Larsson-Raznikiewicz, M.; Schierbeck, B.
Activation and inhibition of the phosphoglycerate kinase reaction by ATP
Biochim. Biophys. Acta
481
283-287
1977
Saccharomyces cerevisiae
brenda
Khamis, M.M.; Larsson-Raznikiewicz, M.
Activation and inhibition of phosphoglycerate kinase by sulphate ion
Biochim. Biophys. Acta
657
190-194
1981
Saccharomyces cerevisiae
brenda
Larsson-Raznikiewicz, M.; Arvidsson, L.
Inhibition of phosphoglycerate kinase by products and product homologues
Eur. J. Biochem.
22
506-512
1971
Saccharomyces cerevisiae
brenda
Larsson-Raznikiewicz, M.; Wiksell, E.
Inhibition of phosphoglycerate kinase by salicylates
Biochim. Biophys. Acta
523
94-100
1978
Saccharomyces cerevisiae
brenda
Boyle, H.A.; Fairbrother, W.J.; Williams, R.J.P.
An NMR analysis of the binding of inhibitors to yeast phosphoglycerate kinase
Eur. J. Biochem.
184
535-543
1989
Saccharomyces cerevisiae
brenda
Scopes, R.K.
3-Phosphoglycerate kinase
The Enzymes, 3rd. Ed. (Boyer, P. D. , ed. )
8
335-351
1973
Saccharomyces cerevisiae, Cyprinus carpio, Oryctolagus cuniculus, Equus caballus, Esox sp., Frog, Homo sapiens, Pisum sativum, Sus scrofa, Testudinidae
-
brenda
Joao, H.C.; Williams, R.J.P.
The anatomy of a kinase and the control of phosphate transfer
Eur. J. Biochem.
216
1-18
1993
Saccharomyces cerevisiae, Equus caballus, Sus scrofa
brenda
Kuntz, G.W.K.; Krietsch, W.K.G.
Phosphoglycerate kinase from spinach, blue-green algae, and yeast
Methods Enzymol.
90
110-114
1982
Saccharomyces cerevisiae, Spinacia oleracea, Spirulina geitleri, Arthrospira platensis
-
brenda
Kulbe, K.D.; Bojanovski, M.
3-Phosphoglycerate kinase from bovine liver and yeast
Methods Enzymol.
90
115-120
1982
Bos taurus, Saccharomyces cerevisiae
-
brenda
Scopes, R.K.
3-Phosphoglycerate kinase of baker's yeast
Methods Enzymol.
42C
134-138
1975
Saccharomyces cerevisiae
-
brenda
Fifis, T.; Scopes, R.K.
Purification of 3-phosphoglycerate kinase from diverse sources by affinity elution chromatography
Biochem. J.
175
311-319
1978
Abramis brama, Beta vulgaris, Bos taurus, Saccharomyces cerevisiae, Bufo vulgaris, Cyprinus carpio, Gallus gallus, Chrysophrys guttulatus, Columba sp., Oryctolagus cuniculus, Dromaius novaehollandiae, Escherichia coli, Equus caballus, Ovis aries, Macropus fuliginosus, Macropus giganteus, Oncorhynchus mykiss, Pseudocheirus peregrinus, Rattus norvegicus, Salmo trutta, Spinacia oleracea, Sus scrofa, Thylogale billardierii, Trichosurus vulpecula, Vombatus ursinus
brenda
Ritco-Vonsovici, M.; Mouratou, B.; Minard, P.; Desmadril, M.; Yon, J.M.; Andrieux, M.; Leroy, E.; Guittet, E.
Role of the C-terminal helix in the folding and stability of yeast phosphoglycerate kinase
Biochemistry
34
833-841
1995
Saccharomyces cerevisiae
brenda
McHarg, J.; Littlechild, J.A.
Studies with inhibitors of the glycolytic enzyme phosphoglycerate kinase for potential treatment of cardiovascular and respiratory disorders
J. Pharm. Pharmacol.
48
201-205
1996
Saccharomyces cerevisiae, Homo sapiens
brenda
Sherman, M.A.; Chen, Y.; Mas, M.T.
An engineered amino-terminal domain of yeast phosphoglycerate kinase with native-like structure
Protein Sci.
6
882-891
1997
Saccharomyces cerevisiae
brenda
McHarg, J.; Kelly, S.M.; Price, N.C.; Cooper, A.; Littlechild, J.A.
Site-directed mutagenesis of proline 204 in the 'hinge' region of yeast phosphoglycerate kinase
Eur. J. Biochem.
259
939-945
1999
Saccharomyces cerevisiae
brenda
Ogino, T.; Iwama, M.; Kinouchi, J.; Shibagaki, Y.; Tsukamoto, T.; Mizumoto, K.
Involvement of a cellular glycolytic enzyme, phosphoglycerate kinase, in Sendai virus transcription
J. Biol. Chem.
274
35999-36008
1999
Bos taurus, Saccharomyces cerevisiae, Oryctolagus cuniculus, Homo sapiens (P00558), Homo sapiens
brenda
Tougard, P.; Bizebard, T.; Ritco-Vonsovici, M.; Minard, P.; Desmadril, M.
Structure of a circularly permuted phosphoglycerate kinase
Acta Crystallogr. Sect. D
58
2018-2023
2002
Saccharomyces cerevisiae (P00560), Saccharomyces cerevisiae
brenda
Tougard, P.; Le, T.H.; Minard, P.; Desmadril, M.; Yon, J.M.; Bizebard, T.; Lebras, G.; Dumas, C.
Structural and functional properties of mutant Arg203Pro from yeast phosphoglycerate kinase, as a model of phosphoglycerate kinase-Uppsala
Protein Eng.
9
181-187
1996
Saccharomyces cerevisiae, Homo sapiens
brenda
Krishnan, P.; Fu, Q.; Lam, W.; Liou, J.Y.; Dutschman, G.; Cheng, Y.C.
Phosphorylation of pyrimidine deoxynucleoside analog diphosphates: selective phosphorylation of L-nucleoside analog diphosphates by 3-phosphoglycerate kinase
J. Biol. Chem.
277
5453-5459
2002
Saccharomyces cerevisiae, Homo sapiens
brenda
Varga, A.; Flachner, B.; Graczer, E.; Osvath, S.; Szilagyi, A.N.; Vas, M.
Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase
FEBS J.
272
1867-1885
2005
Saccharomyces cerevisiae, Sus scrofa
brenda
Balog, E.; Laberge, M.; Fidy, J.
The influence of interdomain interactions on the intradomain motions in yeast phosphoglycerate kinase: a molecular dynamics study
Biophys. J.
92
1709-1716
2007
Saccharomyces cerevisiae (P00560), Saccharomyces cerevisiae
brenda
Hurth, C.; Tassius, C.; Talbot, J.C.; Maali, A.; Moskalenko, C.; Minard, P.; Aime, J.P.; Argoul, F.
Enzymatic activity of immobilized yeast phosphoglycerate kinase
Biosens. Bioelectron.
22
2449-2455
2007
Saccharomyces cerevisiae (P00560), Saccharomyces cerevisiae
brenda
Osvath, S.; Herenyi, L.; Zavodszky, P.; Fidy, J.; Koehler, G.
Hierarchic finite level energy landscape model: to describe the refolding kinetics of phosphoglycerate kinase
J. Biol. Chem.
281
24375-24380
2006
Saccharomyces cerevisiae
brenda
Kotsikorou, E.; Sahota, G.; Oldfield, E.
Bisphosphonate inhibition of phosphoglycerate kinase: quantitative structure-activity relationship and pharmacophore modeling investigation
J. Med. Chem.
49
6692-6703
2006
Saccharomyces cerevisiae, Homo sapiens, Trypanosoma brucei (P07378)
brenda
Young, T.A.; Skordalakes, E.; Marqusee, S.
Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability
J. Mol. Biol.
368
1438-1447
2007
Saccharomyces cerevisiae, Escherichia coli, Escherichia coli (P0A799)
brenda
Osvath, S.; Jackel, M.; Agocs, G.; Zavodszky, P.; Kohler, G.; Fidy, J.
Domain interactions direct misfolding and amyloid formation of yeast phosphoglycerate kinase
Proteins Struct. Funct. Bioinform.
62
909-917
2006
Saccharomyces cerevisiae
brenda
Ijeoma, O.; Hollowell, H.N.; Bodnar, M.A.; Britt, B.M.
Thermodynamic analysis of the nondenaturational conformational change of bakers yeast phosphoglycerate kinase at 24C
Arch. Biochem. Biophys.
478
206-211
2008
Saccharomyces cerevisiae
brenda
White, E.M.; Holland, A.R.; MacDonald, G.
Infrared studies reveal unique vibrations associated with the PGK-ATP-3-PG ternary complex
Biochemistry
47
84-91
2008
Saccharomyces cerevisiae
brenda
Osvath, S.; Quynh, L.M.; Smeller, L.
Thermodynamics and kinetics of the pressure unfolding of phosphoglycerate kinase
Biochemistry
48
10146-10150
2009
Saccharomyces cerevisiae
brenda
Encalada, R.; Rojo-Dominguez, A.; Rodriguez-Zavala, J.S.; Pardo, J.P.; Quezada, H.; Moreno-Sanchez, R.; Saavedra, E.
Molecular basis of the unusual catalytic preference for GDP/GTP in Entamoeba histolytica 3-phosphoglycerate kinase
FEBS J.
276
2037-2047
2009
Entamoeba histolytica, Entamoeba histolytica HM1:IMSS, Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Mazzoni, C.; Torella, M.; Petrera, A.; Palermo, V.; Falcone, C.
PGK1, the gene encoding the glycolitic enzyme phosphoglycerate kinase, acts as a multicopy suppressor of apoptotic phenotypes in S. cerevisiae
Yeast
26
31-37
2009
Saccharomyces cerevisiae
brenda
McCormick, N.E.; Forget, S.M.; Syvitski, R.T.; Jakeman, D.L.
MgF3- and AlF4- transition state analogue complexes of yeast phosphoglycerate kinase
Biochem. Cell Biol.
95
295-303
2017
Saccharomyces cerevisiae
brenda
Li, Q.; Scholl, Z.N.; Marszalek, P.E.
Unraveling the mechanical unfolding pathways of a multidomain protein phosphoglycerate kinase
Biophys. J.
115
46-58
2018
Saccharomyces cerevisiae (P00560), Saccharomyces cerevisiae, Escherichia coli (P0A799), Escherichia coli
brenda
Jin, C.; Zhu, X.; Wu, H.; Wang, Y.; Hu, X.
Perturbation of phosphoglycerate kinase 1 (PGK1) only marginally affects glycolysis in cancer cells
J. Biol. Chem.
295
6425-6446
2020
Saccharomyces cerevisiae, Homo sapiens (P00558), Homo sapiens
brenda
Kouril, T.; Eicher, J.J.; Siebers, B.; Snoep, J.L.
Phosphoglycerate kinase acts as a futile cycle at high temperature
Microbiology
163
1604-1612
2017
Saccharomyces cerevisiae, Saccharolobus solfataricus
brenda
Rojas-Pirela, M.; Andrade-Alviarez, D.; Rojas, V.; Kemmerling, U.; Caceres, A.J.; Michels, P.A.; Concepcion, J.L.; Quinones, W.
Phosphoglycerate kinase structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea
Open Biology
10
200302
2020
Geobacillus stearothermophilus, Corynebacterium glutamicum, Oryctolagus cuniculus, Leishmania mexicana mexicana, Phaeodactylum tricornutum, Spinacia oleracea, Spirulina geitleri, Synechocystis sp. PCC 6803, Thermotoga maritima, Zymomonas mobilis, Trypanosoma rangeli (A0A061J5A1), Trypanosoma rangeli (A0A061J9D5), Entamoeba histolytica (N9V9W5), Homo sapiens (P00558), Saccharomyces cerevisiae (P00560), Trypanosoma brucei brucei (P07377), Trypanosoma brucei brucei (P07378), Thermus thermophilus (P09403), Leishmania major (Q27683), Trypanosoma cruzi (Q4D192), Trypanosoma cruzi (Q4D193), Trypanosoma cruzi, Pseudomonas sp. 'TAC II 18' (Q9RBS3), Entamoeba histolytica HM-1:IMSS-A (N9V9W5), Trypanosoma cruzi CL-Brener (Q4D192), Trypanosoma cruzi CL-Brener (Q4D193), Trypanosoma rangeli SC58 (A0A061J5A1), Trypanosoma rangeli SC58 (A0A061J9D5)
brenda