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Information on EC 2.7.1.44 - galacturonokinase for references in articles please use BRENDA:EC2.7.1.44
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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
alpha-D-galacturonic acid kinase, alpha-D-galacturonic acid-1-phosphate kinase, D-galacturonic acid kinase, GalAK, kinase, galacturono- (phosphorylating),
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alpha-D-galacturonic acid kinase
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alpha-D-galacturonic acid-1-phosphate kinase
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D-galacturonic acid kinase
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kinase, galacturono- (phosphorylating)
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ATP + D-galacturonate = ADP + 1-phospho-alpha-D-galacturonate
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phospho group transfer
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ATP:D-galacturonate 1-phosphotransferase
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ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
D-galacturonate + ATP
1-phospho-alpha-D-galacturonate + ADP
wild-type protein: no activity with D-galactose, D-glucose, D-fructose, D-mannose, D-gluconic acid, D-xylose, N-acetyl-D-galactosamine, N-acetyl-D-glucosamine, D-glucosamine, D-arabinose, L-arabinose, L-rhamnose,or L-Fucose, these monosaccharides (4 mM) have no effect on activity in the presence of galacturonic acid, neither CTP, GTP ITP,TTP, nor UTP are substrates
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?
additional information
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ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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?
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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involved in formation of pectin
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ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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?
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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involved in formation of pectin
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ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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?
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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involved in formation of pectin
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ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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?
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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involved in formation of pectin
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ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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?
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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involved in formation of pectin
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additional information
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D-glucuronic acid, D-galactose and L-arabinose are no substrates, ATP cannot be replaced by other nucleotides
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additional information
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D-glucuronic acid, D-galactose and L-arabinose are no substrates, ATP cannot be replaced by other nucleotides
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additional information
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D-glucuronic acid, D-galactose and L-arabinose are no substrates, ATP cannot be replaced by other nucleotides
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additional information
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D-glucuronic acid, D-galactose and L-arabinose are no substrates, ATP cannot be replaced by other nucleotides
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additional information
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D-glucuronic acid, D-galactose and L-arabinose are no substrates, ATP cannot be replaced by other nucleotides
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ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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involved in formation of pectin
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ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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involved in formation of pectin
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ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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involved in formation of pectin
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ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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involved in formation of pectin
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ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
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involved in formation of pectin
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Co2+
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divalent metal ion is required, lower activity than Mg2+ or Mn2+
Co2+
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divalent metal ion is required, lower activity than Mg2+ or Mn2+
Co2+
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divalent metal ion is required, lower activity than Mg2+ or Mn2+
Co2+
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divalent metal ion is required, lower activity than Mg2+ or Mn2+
Co2+
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divalent metal ion is required, lower activity than Mg2+ or Mn2+
Mg2+
Mn2+ (32% relative activity) and Ca2+ (61% relative activity) can substitute for Mg2+
Mg2+
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divalent metal ion is required, Zn2+ or Ni2+ are ineffective
Mg2+
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divalent metal ion is required, Zn2+ or Ni2+ are ineffective
Mg2+
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divalent metal ion is required, Zn2+ or Ni2+ are ineffective
Mg2+
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divalent metal ion is required, Zn2+ or Ni2+ are ineffective
Mg2+
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divalent metal ion is required, Zn2+ or Ni2+ are ineffective
Mn2+
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divalent metal ion is required, higher activity than Mg2+. Zn2+ or Ni2+ are ineffective
Mn2+
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divalent metal ion is required, higher activity than Mg2+. Zn2+ or Ni2+ are ineffective
Mn2+
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divalent metal ion is required, higher activity than Mg2+. Zn2+ or Ni2+ are ineffective
Mn2+
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divalent metal ion is required, higher activity than Mg2+. Zn2+ or Ni2+ are ineffective
Mn2+
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divalent metal ion is required, higher activity than Mg2+. Zn2+ or Ni2+ are ineffective
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ADP
addition (4 mM) results in 40% reduction of activity
additional information
no inhibition is observed by CTP, GTP ITP,TTP, or UTP (4 mM)
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0.195
ATP
wild-type protein
0.0708 - 0.395
D-galacturonate
0.0708
D-galacturonate
wild-type protein
0.395
D-galacturonate
Y250F mutant protein
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0.76
Alpha-D-glucuronic acid
Y250F mutant protein
6.3
ATP
wild-type protein
24
D-galacturonate
Y250F mutant protein
36
D-galacturonate
wild-type protein
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37
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Uniprot
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buckwheat
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parsley
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pea
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radish
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mung bean
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brenda
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brenda
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brenda
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germinating
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germinating
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germinating
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GALAK_ARATH
424
0
45729
Swiss-Prot
A0A5B7BM31_DAVIN
435
0
47396
TrEMBL
A0A2P6QSA1_ROSCH
429
0
46945
TrEMBL
A0A2G9H5L0_9LAMI
424
0
46457
TrEMBL
G7LJJ0_MEDTR
437
0
48034
TrEMBL
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A386S
possibly critical role in catalysis, relative activity: 90% (wild-type: 100%)
A41E
possibly critical for sugar binding, relative activity: 0% (wild-type: 100%)
Y250F
possibly important for substrate specificity (galacturonic acid /glucuronic acid), relative activity: 90% (wild-type: 100%), 50% activity with D-glucuronic acid (wild-type: 0%)
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mercaptoethanol, 0.05 M, is necessary for preservation of activity in dialysis buffer, lowering its concentration to 0.01 M reduces enzyme activity by 30 to 50%, omission of mercaptoethanol results in complete loss of activity
mercaptoethanol, 0.05 M, is necessary for preservation of activity in dialysis buffer, lowering its concentration to 0.01 M reduces enzyme activity by 30 to 50%, omission of mercaptoethanol results in complete loss of activity
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mercaptoethanol, 0.05 M, is necessary for preservation of activity in dialysis buffer, lowering its concentration to 0.01 M reduces enzyme activity by 30 to 50%, omission of mercaptoethanol results in complete loss of activity
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mercaptoethanol, 0.05 M, is necessary for preservation of activity in dialysis buffer, lowering its concentration to 0.01 M reduces enzyme activity by 30 to 50%, omission of mercaptoethanol results in complete loss of activity
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mercaptoethanol, 0.05 M, is necessary for preservation of activity in dialysis buffer, lowering its concentration to 0.01 M reduces enzyme activity by 30 to 50%, omission of mercaptoethanol results in complete loss of activity
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mercaptoethanol, 0.05 M, is necessary for preservation of activity in dialysis buffer, lowering its concentration to 0.01 M reduces enzyme activity by 30 to 50%, omission of mercaptoethanol results in complete loss of activity
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-20°C, crude recombinant enzyme is stable
-20°C, purified enzyme preparations lose more than 90% of activity within one week
-80°C, stable for several months when diluted with glycerol to 25% (v/v) and flash-frozen in liquid nitrogen
4°C, 0.05 M mercaptoethanol, stable up to 10 days
4°C, 0.05 M mercaptoethanol, stable up to 10 days
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4°C, 0.05 M mercaptoethanol, stable up to 10 days
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4°C, 0.05 M mercaptoethanol, stable up to 10 days
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4°C, 0.05 M mercaptoethanol, stable up to 10 days
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4°C, 0.05 M mercaptoethanol, stable up to 10 days
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partial
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His-tag, expressed in Escherichia coli BL21(de3)plysS
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Neufeld, E.F.; Feingold, D.S.; Ilves, S.M.; Kessler, G.; Hassid, W.Z.
Phosphorylation of D-galacturonic acid by extracts from germinating seeds of Phaseolus aureus
J. Biol. Chem.
236
3102-3105
1961
Fagopyrum esculentum, Petroselinum crispum, Pisum sativum, Raphanus sativus, Vigna radiata var. radiata
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Yang, T.; Bar-Peled, L.; Gebhart, L.; Lee, S.G.; Bar-Peled, M.
Identification of galacturonic acid-1-phosphate kinase, a new member of the GHMP kinase superfamily in plants, and comparison with galactose-1-phosphate kinase
J. Biol. Chem.
284
21526-21535
2009
Arabidopsis thaliana (Q8VYG2)
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2.7.1.44 galacturonokinase
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