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ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
r
ATP + Bacillus subtilis [isocitrate dehydrogenase (NADP+)]
ADP + Bacillus subtilis [isocitrate dehydrogenase (NADP+)] phosphate
-
BsIDH is a much poorer substrate for the enzyme than EcIDH
-
-
?
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
ATP + [isocitrate dehydrogenase (NADP+)]IS
ADP + [isocitrate dehydrogenase (NADP+)]IS phosphate
-
-
-
-
?
ATP + [isocitrate dehydrogenase (NADP+)]N115L
ADP + [isocitrate dehydrogenase (NADP+)]N115L phosphate
-
-
-
-
?
ATP + [isocitrate dehydrogenase (NADP+)]N15L
[isocitrate dehydrogenase (NADP+)]N15L phosphate
-
-
-
-
?
additional information
?
-
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
-
?
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
?
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
?
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
phosphorylation of isocitrate dehydrogenase during growth on acetate is to render this enzyme rate-limiting in the citric acid cycle, this should cause an increase in the level of isocitrate and divert the flux of carbon through the glyoxylate bypass
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
phosphorylation of isocitrate dehydrogenase during growth on acetate is to render this enzyme rate-limiting in the citric acid cycle, this should cause an increase in the level of isocitrate and divert the flux of carbon through the glyoxylate bypass
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
controls the oxidative metabolism, exibits a high intrinsic ATPase activity
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
Escherichia coli AceK can cross-phosphorylate Burkholderia pseudomallei IDH
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
Ser113 from Escherichia coli class A ICDH is the target of phosphorylation by AceK and is structurally conserved among all ICDHs. Burkholderia pseudomallei class A ICDH also exhibits the necessary structural elements required for Escherichia coli AceK recognition
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
The substrate recognition loop of AceK binds to the ICDH dimer, allowing higher order substrate recognition and interaction, and inducing critical conformational change at the phosphorylation site of ICDH
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
isocitrate dehydrogenase kinase/phosphatase (AceK) is a bifunctional enzyme with both kinase and phosphatase activities
-
-
?
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
isocitrate dehydrogenase (NADP+) from Acinetobacter baumannii (AbIDH1) is a substrate for the enzyme (IDHKP) from Escherichia coli. The conserved Ser113 of AbIDH1 is phosphorylated
-
-
?
additional information
?
-
-
uses only ATP, no other nucleoside triphospates as only very poor phosphate donors for the kinase activity, GTP and UTP can activate the phosphatase activity to some extent
-
-
?
additional information
?
-
-
AceK is a bifunctional enzyme, that phosphorylates and dephosphorylates isocitrate dehydrogenase with its unique active site that harbours both the kinase and ATP/ADP-dependent phosphatase activities
-
-
?
additional information
?
-
-
AceK exhibits ATPase activity
-
-
?
additional information
?
-
-
AceK kinase assay is coupled to ICDH activity, whereby the reduction of NADP+ to NADPH is monitored. When AceK phosphorylates ICDH, the activity of ICDH is inhibited. Structure comparisons of Burkholderia pseudomallei ICDH and Echerichia coli ICDH substrates, overview. Bacillus subtilis ICDH and Acidithiobacillus thiooxidans ICDH are poor substrates for AceK
-
-
?
additional information
?
-
bifunctional AceK possesses the two opposing activities of protein kinase and phosphatase within one protein, and specifically recognizes only intact ICDH. Additionally, AceK has strong ATPase activity
-
-
?
additional information
?
-
-
bifunctional AceK possesses the two opposing activities of protein kinase and phosphatase within one protein, and specifically recognizes only intact ICDH. Additionally, AceK has strong ATPase activity
-
-
?
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ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
additional information
?
-
-
AceK is a bifunctional enzyme, that phosphorylates and dephosphorylates isocitrate dehydrogenase with its unique active site that harbours both the kinase and ATP/ADP-dependent phosphatase activities
-
-
?
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
-
?
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
?
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
phosphorylation of isocitrate dehydrogenase during growth on acetate is to render this enzyme rate-limiting in the citric acid cycle, this should cause an increase in the level of isocitrate and divert the flux of carbon through the glyoxylate bypass
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
phosphorylation of isocitrate dehydrogenase during growth on acetate is to render this enzyme rate-limiting in the citric acid cycle, this should cause an increase in the level of isocitrate and divert the flux of carbon through the glyoxylate bypass
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
controls the oxidative metabolism, exibits a high intrinsic ATPase activity
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
Escherichia coli AceK can cross-phosphorylate Burkholderia pseudomallei IDH
-
-
r
ATP + [isocitrate dehydrogenase (NADP+)]
ADP + [isocitrate dehydrogenase (NADP+)] phosphate
isocitrate dehydrogenase kinase/phosphatase (AceK) is a bifunctional enzyme with both kinase and phosphatase activities
-
-
?
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0.0049 - 0.0582
Bacillus subtilis [isocitrate dehydrogenase (NADP+)]
-
0.00023 - 0.0059
[isocitrate dehydrogenase (NADP+)]
0.02
[isocitrate dehydrogenase (NADP+)]IS
-
pH 7.5, 37°C
-
0.0009
[isocitrate dehydrogenase (NADP+)]N15L
-
pH 7.5, 37°C
-
0.0069
ATP
pH 7.5, 37°C, wild-type
0.0087
ATP
pH 7.5, 37°C, mutant D403A
0.0098
ATP
pH 7.5, 37°C, mutant Glu439Ala
0.0147
ATP
pH 7.5, 37°C, mutant Asn377Ala
0.016
ATP
-
pH 7.5, 37°C, wild-type, kinase activity
0.1
ATP
-
pH 7.5, 37°C, mutant AceK3, kinase activity
0.32
ATP
-
pH 7.5, 37°C, mutant AceK4, kinase activity
0.0049
Bacillus subtilis [isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37°C
-
0.0582
Bacillus subtilis [isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37°C, kinase activity at saturating ATP
-
0.00023
[isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37°C, wild-type and mutant AceK4, kinase activity
0.00025
[isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37°C, mutant AceK3, kinase activity
0.00035
[isocitrate dehydrogenase (NADP+)]
-
pH 7.3, 37°C, kinase activity
0.00078
[isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37°C, kinase activity at saturating ATP
0.0017
[isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37°C
0.0026
[isocitrate dehydrogenase (NADP+)]
at pH 7.0 and 37°C
0.0059
[isocitrate dehydrogenase (NADP+)]
-
pH 7.5, 37°C
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1 - 20
3-phosphoglycerate
0.023
DL-isocitrate
-
pH 7.3, 37°C
0.55
phosphoenolpyruvate
-
pH 7.3, 37°C
1
3-phosphoglycerate
-
pH 7.5, 37°C, wild-type, kinase activity
4
3-phosphoglycerate
-
pH 7.5, 37°C, mutant AceK4, kinase activity
20
3-phosphoglycerate
-
pH 7.5, 37°C, mutant AceK3, kinase activity
0.008
AMP
-
pH 7.5, 37°C
0.02
AMP
-
pH 7.5, 37°C, mutant AceK4, kinase activity
0.17
AMP
-
pH 7.5, 37°C, mutant AceK3, kinase activity
0.011
isocitrate
-
pH 7.5, 37°C, mutant AceK4, kinase activity
0.015
isocitrate
-
pH 7.5, 37°C, mutant AceK3, kinase activity
0.016
isocitrate
-
pH 7.5, 37°C, wild-type, kinase activity
0.042
NADPH
-
pH 7.3, 37°C
0.058
NADPH
-
pH 7.5, 37°C, mutant AceK4, kinase activity
0.073
NADPH
-
pH 7.5, 37°C, mutant AceK3, kinase activity
0.082
NADPH
-
pH 7.5, 37°C, wild-type, kinase activity
0.2
pyruvate
-
pH 7.5, 37°C, wild-type, kinase activity
1
pyruvate
-
pH 7.5, 37°C, mutant AceK4, kinase activity
4
pyruvate
-
pH 7.5, 37°C, mutant AceK3, kinase activity
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evolution
AceK is significantly larger than typical eukaryotic protein kinases. Apart from the ATP-binding motif, AceK does not share sequence homology with any eukaryotic protein kinase or phosphatase
evolution
-
the highly stringent AceK binding sites on ICDH are maintained only in Gram-negative bacteria
evolution
-
the N-terminal domain or regulatory domain of AceK represents a unique protein fold with no structural homologues All known and putative AceK proteins exist only in Gram-negative bacteria, close evolutionary relationship among Gram-negative bacterial AceK-IDH systems
metabolism
-
AceK controls the switch between the Krebs cycle and the glyoxylate bypass via regulation of isocitrate dehydrogenase through inactivating phosphorylation and activating dephosphorylation, pathway overview
metabolism
Escherichia coli isocitrate dehydrogenase kinase/phosphatase is a unique bifunctional enzyme that phosphorylates or dephosphorylates isocitrate dehydrogenase, ICDH, in response to environmental changes, resulting in the inactivation or, respectively, activation of ICDH1. ICDH inactivation short-circuits the Krebs cycle by enabling the glyoxlate bypass
physiological function
-
AceK controls the switch between the Krebs cycle and the glyoxylate bypass via regulation of isocitrate dehydrogenase through inactivating phosphorylation and activating dephosphorylation
physiological function
-
isocitrate dehydrogenase kinase/phosphatase, AceK, regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase, ICDH
additional information
-
AceK and its complex with its protein substrate isocitrate dehydrogenase, IDH, interaction analysis, overview. Asp457-Asn462-Asp475 catalytic triad. In addition to this catalytic element, a phosphotransferase motif is also evident in AceK with sequence is 455PGDMLFKNFGV465. One of the most striking differences between AceK and the eukaryotic protein kinases family is the presence of loop beta3aalphaC in AceK. This regulatory loop shields and exposes ATP in the AMP-bound and AMP-free AceK structures, respectively, thereby acting as a regulator of catalytic function as it controls the accessibility to the ATP binding site. The regulatory domain of AceK contains binding pockets for small molecules that can regulate the function of the catalytic kinase domain of AceK
additional information
structures of AceK and its complex with ICDH. AceK contains a eukaryotic protein-kinase-like domain containing ATP and a regulatory domain with a distinct fold. AMP-mediated conformational change exposes and shields ATP, acting as a switch between AceK kinase and phosphatase activities, and ICDH-binding induces further conformational change for AceK activation. The substrate recognition loop of AceK binds to the ICDH dimer, allowing higher order substrate recognition and interaction, and inducing critical conformational change at the phosphorylation site of ICDH, structure-based recognition of Asp 477 being located at the ATP-binding site
additional information
-
structures of AceK and its complex with ICDH. AceK contains a eukaryotic protein-kinase-like domain containing ATP and a regulatory domain with a distinct fold. AMP-mediated conformational change exposes and shields ATP, acting as a switch between AceK kinase and phosphatase activities, and ICDH-binding induces further conformational change for AceK activation. The substrate recognition loop of AceK binds to the ICDH dimer, allowing higher order substrate recognition and interaction, and inducing critical conformational change at the phosphorylation site of ICDH, structure-based recognition of Asp 477 being located at the ATP-binding site
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Nimmo, G.A.; Borthwick, A.C.; Holms, W.H.; Nimmo, H.G.
Partial purification and properties of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli ML308
Eur. J. Biochem.
141
401-408
1984
Escherichia coli
brenda
Nimmo, G.A.; Nimmo, H.G.
The regulatory properties of isocitrate dehydrogenase kinase and isocitrate dehydrogenase phosphatase from Escherichia coli ML308 and the roles of these activities in the control of isocitrate dehydrogenase
Eur. J. Biochem.
141
409-414
1984
Escherichia coli
brenda
Varela, I.; Nimmo, H.G.
Photoaffinity labelling shows that Escherichia coli isocitrate dehydrogenase kinase/phosphatase contains a single ATP-binding site
FEBS Lett.
231
361-365
1988
Escherichia coli, Escherichia coli KAT-1/pEM9
brenda
Ikeda, T.P.; Houtz, E.; LaPorte, D.C.
Isocitrate dehydrogenase kinase/phosphatase: identification of mutations which selectively inhibit phosphatase activity
J. Bacteriol.
174
1414-1416
1992
Escherichia coli, Escherichia coli W3550
brenda
Miller, S.P.; Karschnia, E.J.; Ikeda, T.P.; LaPorte, D.C.
Isocitrate dehydrogenase kinase/phosphatase. Kinetic characteristics of the wild-type and two mutant proteins
J. Biol. Chem.
271
19124-19128
1996
Escherichia coli, Escherichia coli ST2010R
brenda
Rittinger, K.; Negre, D.; Divita, G.; Scarabel, M.; Bonod-Bidaud, C.; Goody, R.S.; Cozzone, A.J.; Cortay, J.C.
Escherichia coli isocitrate dehydrogenase kinase/phosphatase. Overproduction and kinetics of interaction with its substrates by using intrinsic fluorescence and fluorescent nucleotide analogues
Eur. J. Biochem.
237
247-254
1996
Escherichia coli
brenda
El-Mansi, E.M.T.
Control of metabolic interconversion of isocitrate dehydrogenase between the catalytically active and inactive forms in Escherichia coli
FEMS Microbiol. Lett.
166
333-339
1998
Escherichia coli
brenda
Oudot, C.; Jaquinod, M.; Cortay, J.C.; Cozzone, A.J.; Jault, J.M.
The isocitrate dehydrogenase kinase/phosphatase from Escherichia coli is highly sensitive to in-vitro oxidative conditions role of cysteine67 and cysteine108 in the formation of a disulfide-bonded homodimer
Eur. J. Biochem.
262
224-229
1999
Escherichia coli, Escherichia coli JM109
brenda
Miller, S.P.; Chen, R.; Karschnia, E.J.; Romfo, C.; Dean, A.; LaPorte, D.C.
Locations of the regulatory sites for isocitrate dehydrogenase kinase/phosphatase
J. Biol. Chem.
275
833-839
2000
Escherichia coli
brenda
Oudot, C.; Cortay, J.C.; Blanchet, C.; Laporte, D.C.; Di Pietro, A.; Cozzone, A.J.; Jault, J.M.
The "catalytic" triad of isocitrate dehydrogenase kinase/phosphatase from E. coli and its relationship with that found in eukaryotic protein kinases
Biochemistry
40
3047-3055
2001
Escherichia coli (P11071), Escherichia coli, Escherichia coli JM109 (P11071)
brenda
Singh, S.K.; Matsuno, K.; LaPorte, D.C.; Banaszak, L.J.
Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase
J. Biol. Chem.
276
26154-26163
2001
Escherichia coli
brenda
Singh, S.K.; Miller, S.P.; Dean, A.; Banaszak, L.J.; LaPorte, D.C.
Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for Escherichia coli isocitrate dehydrogenase kinase/phosphatase
J. Biol. Chem.
277
7567-7573
2002
Escherichia coli
brenda
Cozzone, A.J.; El-Mansi, M.
Control of isocitrate dehydrogenase catalytic activity by protein phosphorylation in Escherichia coli
J. Mol. Microbiol. Biotechnol.
9
132-146
2005
Escherichia coli
brenda
Yates, S.P.; Edwards, T.E.; Bryan, C.M.; Stein, A.J.; Van Voorhis, W.C.; Myler, P.J.; Stewart, L.J.; Zheng, J.; Jia, Z.
Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase
Biochemistry
50
8103-8106
2011
Burkholderia pseudomallei (Q63Y16), Escherichia coli
brenda
Zheng, J.; Jia, Z.
Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase
Nature
465
961-965
2010
Escherichia coli (Q8X607), Escherichia coli, Escherichia coli 0157:H7 (Q8X607)
brenda
Zheng, J.; Yates, S.P.; Jia, Z.
Structural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK
Philos. Trans. R. Soc. Lond. B Biol. Sci.
367
2656-2668
2012
Escherichia coli
brenda
Yin, Y.; Li, S.; Gao, Y.; Tong, L.; Zheng, J.; Jia, Z.; Jiang, G.; Wei, Q.
Loopbeta3alphaC plays an important role in the structure and function of isocitrate dehydrogenase kinase/phosphatase
FEBS Lett.
590
3144-3154
2016
Escherichia coli (P08200)
brenda
Song, P.; Wang, M.; Zheng, Q.; Wang, P.; Zhu, G.
Isocitrate dehydrogenase 1 from Acinetobacter baummanii (AbIDH1) enzymatic characterization and its regulation by phosphorylation
Biochimie
181
77-85
2021
Escherichia coli
brenda
Yin, Y.; Gao, Y.; Li, S.; Jiang, G.; Wei, Q.
Studies on the activation of isocitrate dehydrogenase kinase/phosphatase (AceK) by Mn2+ and Mg2
Biometals
31
991-1002
2018
Escherichia coli (Q8X607)
brenda