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Information on EC 2.7.1.165 - glycerate 2-kinase and Organism(s) Escherichia coli and UniProt Accession P23524

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IUBMB Comments
A key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea [1,2]. In the bacterium Hyphomicrobium methylovorum GM2 the enzyme is involved in formaldehyde assimilation I (serine pathway) . In Escherichia coli the enzyme is involved in D-glucarate/D-galactarate degradation . The enzyme requires a divalent metal ion .
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This record set is specific for:
Escherichia coli
UNIPROT: P23524
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glycerate kinase (2-phosphoglycerate forming), sso-gk, tm1585, glycerate 2-kinase, class ii glycerate kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-glycerate-2-kinase
-
-
glycerate kinase
SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-glycerate 2-phosphotransferase
A key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea [1,2]. In the bacterium Hyphomicrobium methylovorum GM2 the enzyme is involved in formaldehyde assimilation I (serine pathway) [5]. In Escherichia coli the enzyme is involved in D-glucarate/D-galactarate degradation [6]. The enzyme requires a divalent metal ion [1].
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 + 2-phospho-(R)-glycerate
show the reaction diagram
ATP + D-glycerate
ADP + 2-phospho-(R)-glycerate
show the reaction diagram
-
-
-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL 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 + 2-phospho-(R)-glycerate
show the reaction diagram
-
enzymes in the (D)-glucarate/galactarate catabolic pathway
-
-
?
ATP + D-glycerate
ADP + 2-phospho-(R)-glycerate
show the reaction diagram
-
-
-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.051
(R)-glycerate
-
pH 7.5, 22°C
0.061
ATP
-
pH 7.5, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
(R)-glycerate
-
pH 7.5, 22°C
2.5
ATP
-
pH 7.5, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
development of a microbial production platform in Escherichia coli to synthesize D-glyceric acid from D-galacturonate. The expression of uronate dehydrogenase (udh) from Pseudomonas syringae and galactarolactone isomerase (gli) from Agrobacterium fabrum, along with the inactivation of garK, encoding for glycerate kinase, enables D-glyceric acid accumulation by utilizing the endogenous expression of galactarate dehydratase (garD), 5-keto-4-deoxy-D-glucarate aldolase (garL), and 2-hydroxy-3-oxopropionate reductase (garR). Optimization of carbon flux through the elimination of competing metabolic pathways leads to the development of a DELTAgarKDELTAhyiDELTAglxKDELTAuxaC mutant strain that produces 4.8 g/l of D-glyceric acid from D-galacturonate, with an 83% molar yield. Cultivation in a minimal medium produces similar yields and demonstrates that galactose or glycerol serve as possible carbon co-feeds for industrial production, method overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme does not require dithiothreitol to retain full activity
-
the enzyme retains full activity through at least one freeze–thaw cycle
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, storage buffer containing 1 mM NaN3, enzyme retains full activity through prolonged storage
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hubbard, B.K.; Koch, M.; Palmer, D.R.J.; Babbitt, P.C.; Gerlt, J.A.
Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli
Biochemistry
37
14369-14375
1998
Escherichia coli
Manually annotated by BRENDA team
Sims, P.A
Reed, G.H.: Method for the enzymatic synthesis of 2-phospho-D-glycerate from adenosine 5'-triphosphate and D-glycerate via D-glycerate-2-kinase
J. Mol. Catal. B
32
77-81
2005
Escherichia coli
-
Manually annotated by BRENDA team
Zelcbuch, L.; Razo-Mejia, M.; Herz, E.; Yahav, S.; Antonovsky, N.; Kroytoro, H.; Milo, R.; Bar-Even, A.
An in vivo metabolic approach for deciphering the product specificity of glycerate kinase proves that both E. colis glycerate kinases generate 2-phosphoglycerate
PLoS ONE
10
e0122957
2015
Escherichia coli
Manually annotated by BRENDA team
Fox, K.; Prather, K.
Production of d-Glyceric acid from d-Galacturonate in Escherichia coli
J. Ind. Microbiol. Biotechnol.
47
1075-1081
2020
Escherichia coli (P23524)
Manually annotated by BRENDA team