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Enzyme Nomenclature
Information on EC 2.7.1.44 - galacturonokinase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.7.1.44
-
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RECOMMENDED NAME
GeneOntology No.
galacturonokinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + D-galacturonate = ADP + 1-phospho-alpha-D-galacturonate
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-galacturonate 1-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
9026-63-5
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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-
?
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
-
-
-
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
-
-
-
?
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
-
involved in formation of pectin
-
-
-
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
-
involved in formation of pectin
-
-
-
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
-
involved in formation of pectin
-
-
-
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
-
-
-
?
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
-
involved in formation of pectin
-
-
-
additional information
?
-
-
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
?
-
-
D-glucuronic acid, D-galactose and L-arabinose are no substrates, ATP cannot be replaced by other nucleotides
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-
-
additional information
?
-
-
D-glucuronic acid, D-galactose and L-arabinose are no substrates, ATP cannot be replaced by other nucleotides
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-
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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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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
-
involved in formation of pectin
-
-
-
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
-
involved in formation of pectin
-
-
-
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
-
involved in formation of pectin
-
-
-
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
-
involved in formation of pectin
-
-
-
ATP + D-galacturonate
ADP + 1-phospho-alpha-D-galacturonate
-
involved in formation of pectin
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
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+
-
divalent metal ion is required, Zn2+ or Ni2+ are ineffective
Mn2+
-
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+
-
divalent metal ion is required, higher activity than Mg2+. Zn2+ or Ni2+ are ineffective
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition is observed by CTP, GTP ITP,TTP, or UTP (4 mM)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.1.44)
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