Any feedback?
Information on EC 2.7.2.1 - acetate kinase and Organism(s) Methanosarcina thermophila and UniProt Accession P38502
for references in articles please use BRENDA:EC2.7.2.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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 .
Specify your search results
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: Methanosarcina thermophila
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, urkinase, atp-ecoak, acetic kinase, stacka, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetate kinase (phosphorylating)
-
-
-
-
acetic kinase
-
-
-
-
acetokinase
-
-
-
-
AK
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + acetate = ADP + acetyl phosphate
roles for the arginine residues Arg241 and Arg91 in transition state stabilization for catalysis but not in nucleotide binding determined, experimental evidence for domain motion
ATP + acetate = ADP + acetyl phosphate
residue F179 is essential for catalysis
-
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
-
-
-
r
ATP + propionate
ADP + propionyl phosphate
the enzyme phosphorylates propionate at 60% of the rate with acetate
-
-
?
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
-
-
-
-
r
ATP + ethanol
ADP + ethyl phosphate
-
1% of reactivity with acetate
-
-
r
ATP + formate
ADP + formyl phosphate
-
2% of reactivity with acetate
-
-
r
ATP + glycerol
ADP + glycerol phosphate
-
1% of reactivity with acetate
-
-
r
ATP + glycine
ADP + glycyl phosphate
-
1% of reactivity with acetate
-
-
r
ATP + acetate
ADP + acetyl phosphate
catalytic mechanism, roles for the arginine residues Arg241 and Arg91 in transition state stabilization for catalysis but not in nucleotide binding determined, experimental evidence for domain motion
-
-
r
ATP + acetate
ADP + acetyl phosphate
the enzyme is proposed to function in the initial activation of acetate for conversion to methane and CO2
-
-
?
ATP + acetate
ADP + acetyl phosphate
activity in the reverse direction is 2.6fold greater than in the forward direction (acetate kinase activity)
-
-
r
ATP + acetate
ADP + acetyl phosphate
the wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP
-
-
?
CTP + acetate
CDP + acetyl phosphate
activity with TP is 53% of the activity with ATP
-
-
?
CTP + acetate
CDP + acetyl phosphate
50% of the activity relative to that observed with ATP
-
-
?
GTP + acetate
GDP + acetyl phosphate
activity with TP is 79% of the activity with ATP
-
-
?
GTP + acetate
GDP + acetyl phosphate
85.2% of the activity relative to that observed with ATP
-
-
?
ITP + acetate
IDP + acetyl phosphate
activity with TP is 83% of the activity with ATP
-
-
?
ITP + acetate
IDP + acetyl phosphate
80% of the activity relative to that observed with ATP
-
-
?
TTP + acetate
TDP + acetyl phosphate
activity with TP is 106% of the activity with ATP
-
-
?
TTP + acetate
TDP + acetyl phosphate
64.5% of the activity relative to that observed with ATP
-
-
?
UTP + acetate
UDP + acetyl phosphate
activity with TP is 80% of the activity with ATP
-
-
?
UTP + acetate
UDP + acetyl phosphate
54.8% of the activity relative to that observed with ATP
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
function in the initial activation of acetate for conversion to methane and CO2
-
r
ATP + butyrate
ADP + butyryl phosphate
-
2% of reactivity with acetate
-
-
r
additional information
?
-
the enzyme is unable to use formate
-
-
?
additional information
?
-
-
the enzyme is unable to use formate
-
-
?
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
ATP + acetate
ADP + acetyl phosphate
the enzyme is proposed to function in the initial activation of acetate for conversion to methane and CO2
-
-
?
ATP + acetate
ADP + acetyl phosphate
-
function in the initial activation of acetate for conversion to methane and CO2
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). Cu2+, Ni2+, or Zn2+ resulted in no significanta activity
Co2+
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). Cu2+, Ni2+, or Zn2+ resulted in no significanta activity
Mg2+
Mn2+
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). The maximum rate is obtained with Mn2+
Mg2+
binding constants of enzyme variants with ADP measured
Mg2+
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). Cu2+, Ni2+, or Zn2+ resulted in no significanta activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CDP
preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity
diphosphate
about 70% inhibition in the acetate-forming direction and about 90% inhibition in the acetyl phosphate-forming direction
IDP
preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity
KCl
activity linearly decreases from 100% (at 0 mM added KCl) to 71% at 500 mM added KCl
propionate
preincubation with MgCl2, ADP, AlCl3, NaF, and propionate results in almost complete inhibition of activity
UDP
preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity
acetate
inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity
acetate
inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition)
ADP
inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity
ADP
inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition). The transition state analog, MgADP-aluminum fluoride-acetate, forms an abortive complex in the active site
AlCl3
inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity
AlCl3
inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition). The transition state analog, MgADP-aluminum fluoride-acetate, forms an abortive complex in the active site. Protection from inhibition by a non-hydrolyzable ATP analog or acetylphosphate. Preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity
MgCl2
inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity
MgCl2
inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition). The transition state analog, MgADP-aluminum fluoride-acetate, forms an abortive complex in the active site. Preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity
NaF
inhibition by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate. When MgCl2, ADP, and acetate are omitted from the preincubation mixture, there is no detectable loss of activity
NaF
inhibition of acetate kinase by preincubation with MgCl2, ADP, AlCl3, NaF, and acetate (all of the components are necessary for maximum inhibition). The transition state analog, MgADP-aluminum fluoride-acetate, forms an abortive complex in the active site. Preincubation of acetate kinase with MgCl2, AlCl3, NaF, acetate, and either IDP, UDP, or CDP in place of ADP results in almost complete inhibition of activity
additional information
preincubation with butyrate does not significantly inhibit the enzyme
-
additional information
-
preincubation with butyrate does not significantly inhibit the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
assay methods for both directions of reaction
-
24
acetate
wild-type, pH 7.0, presence of 200 mM guanidine/HCl
30
acetate
mutant R241A, pH 7.0, presence of 200 mM guanidine/HCl
83
acetate
mutant R91A, pH 7.0, presence of 200 mM guanidine/HCl
1.7
acetyl phosphate
mutant enzyme G331Q/I332M, at pH 7.0 and 37°C
0.068
ATP
mutant R91A, pH 7.0, presence of 200 mM guanidine/HCl
0.068
ATP
wild-type, pH 7.0, presence of 200 mM guanidine/HCl
0.264
ATP
mutant R241A, pH 7.0, presence of 200 mM guanidine/HCl
17
acetate
-
pH 7.0, 37°C, mutant H180E, H180N, produced in E. coli
18
acetate
-
pH 7.0, 37°C, unaltered wild-type enzyme, produced in E. coli
1.4
ATP
-
pH 7.0, 20°C, mutants E97A, E97D, E97Q, produced in E. coli
2
ATP
-
pH 7.0, 37°C, unaltered wild-type enzyme, produced in E. coli
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12
acetyl phosphate
mutant enzyme G331Q/I332M, at pH 7.0 and 37°C
1550
acetyl phosphate
wild type enzyme, at pH 7.0 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.057
acetate
mutant enzyme G331Q/I332M, at pH 5.5 and 45°C
7.2
acetyl phosphate
mutant enzyme G331Q/I332M, at pH 7.0 and 37°C
1294
acetyl phosphate
wild type enzyme, at pH 7.0 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.9
acetate
pH and temperature not specified in the publication
2.9
acetate
pH 5.5, temperature not specified in the publication
0.0184
ADP
pH and temperature not specified in the publication
18.4
ADP
pH 5.5, temperature not specified in the publication
0.95
AlCl3
pH and temperature not specified in the publication
3.4
AlCl3
pH 5.5, temperature not specified in the publication
0.95
MgCl2
pH 5.5, temperature not specified in the publication
3.4
MgCl2
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.3
diphosphate
Methanosarcina thermophila
wild type enzyme, in the acetate-forming direction, at pH 7.0 and 37°C
4
diphosphate
Methanosarcina thermophila
mutant enzyme G331Q/I332M, in the acetate-forming direction, at pH 7.0 and 37°C
7.5
diphosphate
Methanosarcina thermophila
wild type enzyme, in the acetyl phosphate-forming direction, at pH 5.5 and 45°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
catalytic mechanism analyzed in wild-type and mutant variants, binding constants for the nucleotide substrates indicate that Arg241 is involved in transition state stabilization and not directly involved in nucleotide recognition or binding, or in the domain closure required for catalysis, binding constants of the nucleotide substrates for Arg91 suggest that this residue has a role in transition state stabilization, evidence for domain motion dependent upon nucleotide ligand binding presented, suggestion that Arg91 is important for closure of domain I onto domain II for catalysis
additional information
-
catalytic mechanism analyzed in wild-type and mutant variants, binding constants for the nucleotide substrates indicate that Arg241 is involved in transition state stabilization and not directly involved in nucleotide recognition or binding, or in the domain closure required for catalysis, binding constants of the nucleotide substrates for Arg91 suggest that this residue has a role in transition state stabilization, evidence for domain motion dependent upon nucleotide ligand binding presented, suggestion that Arg91 is important for closure of domain I onto domain II for catalysis
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
pH 6.0: about 75% of maximal activity, pH 8.5: about 65% of maximal activity, acetate kinase activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is proposed to function in the initial activation of acetate for conversion to methane and CO2
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
three-dimensional structure of Methanosarcina thermophila acetate kinase bound to ADP
space group C2, unit cell dimensions a = 181 A, b = 67 A, c = 83 A, beta 103 degrees
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G239A
14.5fold reduced specific activity (with ATP as substrate). The wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP. The mutant enzyme shows a shift in NTP utilization. It displays substantially higher activity with TTP than with ATP, and activity (as a percentage of that observed with ATP) increased greatly with CTP as well. A weak increase in activity is observed with UTP. Activity with the purines GTP and ITP versus ATP decreases
G239S
192fold reduced specific activity (with ATP as substrate). The wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP. The mutant enzyme shows a shift in NTP utilization. It displays substantially higher activity with TTP than with ATP, and activity (as a percentage of that observed with ATP) increased greatly with CTP as well. A weak increase in activity is observed with UTP. Activity with the purines GTP and ITP versus ATP decreases
G331A
15.2fold reduced specific activity (with ATP as substrate). The wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP. Activity of mutant enzyme with the pyrimidine nucleotides CTP, TTP, and UTP is significantly reduced, with each displaying less than 12% activity versus ATP. Activity with GTP and ITP is also reduced, but to a much lesser extent
G331Q
118fold reduced specific activity. The wild type enzyme shows broad NTP utilization, with greater than 50% activity with CTP, GTP, TTP, UTP, and ITP versus ATP. Activity of mutant enzyme with the pyrimidine nucleotides CTP, TTP, and UTP is significantly reduced, with each displaying less than 12% activity versus ATP. Activity with GTP and ITP is also reduced, but to a much lesser extent
G331Q/I332M
the mutations result in substantial reductions in kcat compared to the wild type enzyme. In the acetate-forming direction, catalysis is reduced over 100fold, and in the acetyl phosphate-forming direction, kcat is reduced about 50fold. This alteration results in about 5fold increase in Km for ADP and ATP, and a 15fold increase in Km for acetate but no substantial change in the Km for acetyl phosphate
N211A
6fold reduced specific activity (with ATP as substrate). The percentage activity observed with CTP and ITP versus ATP is similar to that observed with the wild type enzyme. Activity with GTP and UTP decreases somewhat, and activity with TTP shows an increase
N211S
200fold reduced specific activity (with ATP as substrate). The percentage activity observed with CTP and ITP versus ATP is similar to that observed with the wild type enzyme. Activity with GTP and UTP decreases somewhat, and activity with TTP shows an increase
N211T
44fold reduced specific activity (with ATP as substrate). Mutant enzyme shows little change in percentage activity observed with CTP and ITP. Activity with TTP is greatly enhanced and nearly equal to that observed with ATP, whereas the reduction in activity with UTP is stronger than that observed with the N211A
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
stable for 15 min, rapidly inactivated at higher temperature
70
-
stable to heating for 15 min, but rapidly inactivated at higher temperatures
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
all 4 substrates of the forward and reverse reaction protect the enzyme from inactivation by diethyldicarbonate
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen in liquid nitrogen, the enzyme is stable for at least months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified wild-type and recombinant enzymes, R175L and R340A are unstable and cannot be purified
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant acetate kinase with a 6-residue N-terminal histidine tag is heterologously produced in Escherichia coli BL21(DE3)
wild-type and mutant acetate kinase genes subcloned in to the T7-based expression vector pET15b
-
wild-type and variant acetate kinases are overproduced in Escherichia coli BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Aceti, D.J.; Ferry, J.G.
Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila
J. Biol. Chem.
249
15444-15448
1988
Methanosarcina thermophila
-
Buss, K.A.; Ingram-Smith, C.; Ferry, J.G.; Sanders, D.A.; Hasson, M.S.
Crystallization of acetate kinase from Methanosarcina thermophila and prediction of its fold
Protein Sci.
6
2659-2662
1997
Methanosarcina thermophila
Singh-Wissmann, K.; Ingram-Smith, C.; Miles, R.D.; Ferry, J.G.
Identification of essential glutamates in the acetate kinase from Methanosarcina thermophila
J. Bacteriol.
180
1129-1134
1998
Methanosarcina thermophila
Ingram-Smith, C.; Barber, R.D.; Ferry, J.G.
The role of histidines in the acetate kinase from Methanosarcina thermophila
J. Biol. Chem.
275
33765-33770
2000
Methanosarcina thermophila
Singh-Wissmann, K.; Miles, R.D.; Ingram-Smith, C.; Ferry, J.G.
Identification of essential arginines in the acetate kinase from Methanosarcina thermophila
Biochemistry
39
3671-3677
2000
Methanosarcina thermophila
Miles, R.D.; Iyer, P.P.; Ferry, J.G.
Site-directed mutational analysis of active site residues in the acetate kinase from Methanosarcina thermophila
J. Biol. Chem.
276
45059-45064
2001
Methanosarcina thermophila
Ingram-Smith, C.; Gorrell, A.; Lawrence, S.H.; Iyer, P.; Smith, K.; Ferry, J.G.
Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase
J. Bacteriol.
187
2386-2394
2005
Methanosarcina thermophila
Gorrell, A.; Lawrence, S.H.; Ferry, J.G.
Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila
J. Biol. Chem.
280
10731-10742
2005
Methanosarcina thermophila (P38502), Methanosarcina thermophila
Iyer, P.; Ferry, J.G.
Acetate kinase from Methanosarcina thermophila, a key enzyme for methanogenesis
Methods Biotechnol.
17
239-246
2005
Methanosarcina thermophila
-
Ingram-Smith, C.; Martin, S.R.; Smith, K.S.
Acetate kinase: not just a bacterial enzyme
Trends Microbiol.
14
249-253
2006
Mesoplasma florum, Histoplasma capsulatum, Cupriavidus necator, Aspergillus fumigatus, Aspergillus nidulans, Bacillus subtilis, Borreliella burgdorferi, Chaetomium globosum, Chlamydomonas reinhardtii, Phanerodontia chrysosporium, Coccidioides immitis, Coprinopsis cinerea, Cryptococcus neoformans, Streptococcus pneumoniae, Entamoeba histolytica, Enterococcus faecalis, Salmonella enterica, Fusarium graminearum, Helicobacter pylori, Lactobacillus acidophilus, Lactococcus lactis, Listeria monocytogenes, Pyricularia grisea, Methanosarcina mazei, Methanosarcina thermophila, Staphylococcus aureus, Mycoplasma pneumoniae, Neurospora crassa, Oceanobacillus iheyensis, Phytophthora sojae, Sclerotinia sclerotiorum, Trichoderma reesei, Ustilago maydis, Methanosarcina acetivorans, Parastagonospora nodorum, Uncinocarpus reesii, Phytophthora ramorum
Gorrell, A.; Ferry, J.G.
Investigation of the Methanosarcina thermophila acetate kinase mechanism by fluorescence quenching
Biochemistry
46
14170-14176
2007
Methanosarcina thermophila (P38502), Methanosarcina thermophila
Buss, K.A.; Cooper, D.R.; Ingram-Smith, C.; Ferry, J.G.; Sanders, D.A.; Hasson, M.S.
Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases
J. Bacteriol.
183
680-686
2001
Methanosarcina thermophila (P38502), Methanosarcina thermophila
Aceti, D.J.; Ferry, J.G.
Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila. Evidence for regulation of synthesis
J. Biol. Chem.
263
15444-15448
1988
Methanosarcina thermophila (P38502), Methanosarcina thermophila, Methanosarcina thermophila TM-1 (P38502)
Miles, R.D.; Gorrell, A.; Ferry, J.G.
Evidence for a transition state analog, MgADP-aluminum fluoride-acetate, in acetate kinase from Methanosarcina thermophila
J. Biol. Chem.
277
22547-22552
2002
Methanosarcina thermophila (P38502), Methanosarcina thermophila
Ingram-Smith, C.; Wharton, J.; Reinholz, C.; Doucet, T.; Hesler, R.; Smith, K.
The role of active site residues in ATP binding and catalysis in the Methanosarcina thermophila acetate kinase
Life
5
861-871
2015
Methanosarcina thermophila (P38502), Methanosarcina thermophila
EXTERNAL LINKS (specific for EC-Number 2.7.2.1)
Transporter Classification Database (TCDB): 9.B.75.2.1
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
