Information on EC 2.7.1.31 - glycerate 3-kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.7.1.31
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RECOMMENDED NAME
GeneOntology No.
glycerate 3-kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + D-glycerate = ADP + 3-phospho-D-glycerate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
photorespiration
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glycolate and glyoxylate degradation
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serine metabolism
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Glycine, serine and threonine metabolism
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Glycerolipid metabolism
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Glyoxylate and dicarboxylate metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-glycerate 3-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-61-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Crook's strain, ATCC 8739
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-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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glycerate 3-kinase is the terminal enzyme of the photorespiratory cycle
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (R)-glycerate
ADP + 3-phospho-(R)-glycerate
show the reaction diagram
ATP + D-glycerate
ADP + 3-phospho-D-glycerate
show the reaction diagram
ATP + D-glycerate
ADP + 3-phosphoglycerate
show the reaction diagram
ATP + glycerate
ADP + 3-phospho-(R)-glycerate
show the reaction diagram
GTP + (R)-glycerate
GDP + 3-phospho-(R)-glycerate
show the reaction diagram
UTP + (R)-glycerate
UDP + 3-phospho-(R)-glycerate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-glycerate
ADP + 3-phospho-D-glycerate
show the reaction diagram
ATP + glycerate
ADP + 3-phospho-(R)-glycerate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
divalent cation requirement satisfied by 0.1 M Mg2+ or Co2+ and partially satisfied by Mn2+, Fe2+ or Ca2+
K+
-
stimulation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-phosphoglycerate
ammonium sulfate
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inhibits at high concentrations
fructose 6-phosphate
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weak
Fructose bisphosphates
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-
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glucose 1-phosphate
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weak
glucose 6-phosphate
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weak
iodoacetate
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p-chloromercuribenzoate
p-hydroxymercuribenzoate
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pyruvate
ribose 5-phosphate
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Ribulose 1,5-bisphosphate
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-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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10 mM dithiothreitol activates the enzyme activity about 4fold (but relatively slow)
reduced thioredoxin
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about 3fold activation within 40 min
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13 - 707
ATP
0.104 - 0.45
D-glycerate
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
200 - 350
D-glycerate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21.3
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purified recombinant enzyme
27.9
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purified recombinant enzyme
54.6
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purified native enzyme
68
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additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
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6.8 - 8.5
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7.4 - 7.7
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 8.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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gel filtration
47000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 39000, native enzyme, SDS-PAGE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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stable
641330, 641331
10
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stable below
641330, 641331
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
highly reducing conditions stabilize
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-40C, stable for more than 2 years
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0-4C, 100 mM 2-mercaptoethanol, stable for at least 3 weeks
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4C, highly purified crystalline enzyme, 45% ethanol, stable for several weeks
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purified enzyme totally unstable after overnight storage in a freezer unless bovine serum albumin, 3 mg/ml, is added
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 867fold from leaves by hydrophobic interaction, anion exchange, and 2 steps affinity chromatography, recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
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partial
recombinant His-tagged enzyme from Escherichia coli strain BL21 to homogeneity by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain D5alpha
expressed in Escherichia coli Top10 cells
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functional expression of His-tagged enzyme in Escherichia coli strain BL21, phylogenetic analysis
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single-copy gene, partial DNA and amino acid sequence determination and analysis, functional expression of His-tagged enzyme in Escherichia coli strain BL21, phylogenetic analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme activity is upregulated 10 min after light exposure following 4 h of dark adaptation of leaves
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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construction of inactive T-DNA insertion knockout mutants, which are not viable in normal air, but grow under elevated CO2 concentration, and show high accumulation of glycerate, overview
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