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Information on EC 2.7.2.1 - acetate kinase and Organism(s) Thermotoga maritima and UniProt Accession Q9WYB1
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2.7.2.1 acetate kinaseIUBMB Comments
Requires Mg2+ for activity. While purified enzyme from Escherichia coli is specific for acetate , others have found that the enzyme can also use propanoate as a substrate, but more slowly . Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8, phosphate acetyltransferase. Both this enzyme and EC 2.7.2.15, propionate kinase, play important roles in the production of propanoate .
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Word Map
- 2.7.2.1
- phosphotransacetylase
- acetyl-coa
- cdc42
- methanosarcina
- thermophila
- sludge
-
acetogenic
-
cdc42-associated
- acetylphosphate
- formate-lyase
-
non-receptor
- acetobutylicum
-
substrate-level
- acetoin
- tyrobutyricum
-
adp-forming
- phosphoketolase
- butyryl-coa
-
embden-meyerhof-parnas
-
acetate-activating
- synthesis
- industry
The taxonomic range for the selected organisms is: Thermotoga maritima
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
acetate kinase, ack, acetokinase, acka2, acka1, ackase, atp-ecoak, urkinase, acetic kinase, atp-specific ak, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetate kinase (phosphorylating)
-
-
-
-
acetic kinase
-
-
-
-
acetokinase
-
-
-
-
AK
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:acetate phosphotransferase
Requires Mg2+ for activity. While purified enzyme from Escherichia coli is specific for acetate [4], others have found that the enzyme can also use propanoate as a substrate, but more slowly [7]. Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8, phosphate acetyltransferase. Both this enzyme and EC 2.7.2.15, propionate kinase, play important roles in the production of propanoate [9].
CAS REGISTRY NUMBER
COMMENTARY
9027-42-3
-
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
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
high-energy acetyl phosphate reacts with hydroxylamine forming acetyl hydroxamate and inorganic phosphate
-
-
?
additional information
?
-
-
butyrate, isobutyrate, valerate and isovalerate are no substrates
-
-
?
ATP + acetate
ADP + acetyl phosphate
enzyme assay developed that can measure the released phosphate at a nanomolar level
-
-
?
NATURAL SUBSTRATE
NATURAL 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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hydroxylamine
inhibits acetate kinase reaction in a nonlinear and noncompetitive fashion, substantial inhibition at concentrations of 704 mM and minimal inhibition at concentrations of 250 microM hydroxylamine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
lower Km of the Thermotoga maritima acetate kinase for acetate measured than that determined by earlier assay methods
-
additional information
additional information
-
lower Km of the Thermotoga maritima acetate kinase for acetate measured than that determined by earlier assay methods
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
continuous assay, spectrophotometric quantification of phosphate achieved through measurement of the phosphorylysis of 2-amino-6-mercapto-7-methyl-purine riboside (MESG) to ribose-1-phosphate and 2-amino-6-mercapto-7-methyl-purine (MES) by purine nucleoside phosphorylase, sensitivity of the assay is in the range of 2-150 microM
additional information
-
continuous assay, spectrophotometric quantification of phosphate achieved through measurement of the phosphorylysis of 2-amino-6-mercapto-7-methyl-purine riboside (MESG) to ribose-1-phosphate and 2-amino-6-mercapto-7-methyl-purine (MES) by purine nucleoside phosphorylase, sensitivity of the assay is in the range of 2-150 microM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 100
-
activity increases rapidly above 55°C, enzyme does not lose activity at 80°C upon incubation for 180 min
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55 - 100
-
almost complete loss about 90% is observed after incubation at 100°C for about 60 min, enzyme does not lose activity upon incubation for 3 h at 100°C in presence of 1 M (NH4)2SO4
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilized against heat inactivation by salts, most effective (NH4)2SO4
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, can be stored in 20 mM Tris-HCl, pH 8.0, 2.0 mM MgCl2, 0.32 M NaCl, supplemented with 10% glycerol, without significant loss of activity for several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bock, A.K.; Glasemacher, J.; Schmidt, R.; Schonheit, P.
Purification and characterization of two extremely thermostable enzymes, phosphate acetyltransferase and acetate kinase, from the hyperthermophilic eubacterium Thermotoga maritima
J. Bacteriol.
181
1861-1867
1999
Thermotoga maritima
EXTERNAL LINKS (specific for EC-Number 2.7.2.1)
Transporter Classification Database (TCDB): 9.B.75.2.1
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