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Information on EC 2.7.2.1 - acetate kinase and Organism(s) Methanosarcina thermophila and UniProt Accession P38502

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IUBMB 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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This record set is specific for:
Methanosarcina thermophila
UNIPROT: P38502
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The taxonomic range for the selected organisms is: Methanosarcina thermophila
Synonyms
acetate kinase (phosphorylating), acetic kinase, acetokinase, ACK, ackA, AckA1, AckA2, ACKase, AK, ATP-ecoAK, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetate kinase (phosphorylating)
-
-
-
-
acetic kinase
-
-
-
-
acetokinase
-
-
-
-
ACK
286004
gene name
AK
-
-
-
-
urkinase
286004
amgiguous
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + acetate = ADP + acetyl phosphate
show the reaction diagram
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
show the reaction diagram
residue F179 is essential for catalysis
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
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 hide
9027-42-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + acetate
ADP + acetyl phosphate
show the reaction diagram
ATP + propionate
ADP + propionyl phosphate
show the reaction diagram
-
the enzyme phosphorylates propionate at 60% of the rate with acetate
-
-
?
CTP + acetate
CDP + acetyl phosphate
show the reaction diagram
GTP + acetate
GDP + acetyl phosphate
show the reaction diagram
ITP + acetate
IDP + acetyl phosphate
show the reaction diagram
TTP + acetate
TDP + acetyl phosphate
show the reaction diagram
UTP + acetate
UDP + acetyl phosphate
show the reaction diagram
acetyl phosphate + hydroxylamine
acetyl hydroxamate + phosphate
show the reaction diagram
ATP + acetate
ADP + acetyl phosphate
show the reaction diagram
ATP + butyrate
ADP + butyryl phosphate
show the reaction diagram
ATP + ethanol
ADP + ethyl phosphate
show the reaction diagram
-
1% of reactivity with acetate
-
-
r
ATP + formate
ADP + formyl phosphate
show the reaction diagram
-
2% of reactivity with acetate
-
-
r
ATP + glycerol
ADP + glycerol phosphate
show the reaction diagram
-
1% of reactivity with acetate
-
-
r
ATP + glycine
ADP + glycyl phosphate
show the reaction diagram
-
1% of reactivity with acetate
-
-
r
ATP + glycolic acid
ADP + ?
show the reaction diagram
-
4% of reactivity with acetate
-
-
r
ATP + propionate
ADP + propionyl phosphate
show the reaction diagram
CTP + acetate
CDP + acetyl phosphate
show the reaction diagram
-
-
-
r
GTP + acetate
GDP + acetyl phosphate
show the reaction diagram
-
-
-
r
ITP + acetate
IDP + acetyl phosphate
show the reaction diagram
-
-
-
r
TTP + acetate
TDP + acetyl phosphate
show the reaction diagram
-
-
-
r
additional information
?
-
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 + acetate
ADP + acetyl phosphate
show the reaction diagram
ATP + acetate
ADP + acetyl phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
Mn2+
-
the enzyme requires a divalent cations for activity (Mn2+, Mg2+ Co2+ or Ca2+). The maximum rate is obtained with Mn2+
additional information
-
no activity with Cu2+, Ni2+ or Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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; 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; 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; 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
ATP-gamma-S
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non-hydrolyzable inhibitor
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
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
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; 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; 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
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
adenosine 5'-(gamma-thio)triphosphate
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diethyldicarbonate
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N-ethylmaleimide
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.7 - 601
acetate
0.26 - 2.58
acetyl phosphate
0.098 - 0.692
ADP
0.053 - 18.4
ATP
3.2 - 15.7
CTP
5.3 - 7.4
GTP
4.7 - 10.7
ITP
2.7 - 12.1
TTP
2.7 - 14.2
UTP
1.5 - 1573
acetate
0.15 - 2.3
acetyl phosphate
0.063 - 1.26
ADP
0.016 - 56
ATP
33.4 - 63
Butyrate
6.2 - 46
propionate
additional information
additional information
-
assay methods for both directions of reaction
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.63 - 2650
ADP
0.4 - 913
ATP
2.1 - 460
CTP
8.6 - 571
GTP
11 - 742
ITP
2.8 - 540
TTP
2.8 - 415
UTP
190 - 1042
acetate
12 - 3869
acetyl phosphate
0.42 - 1260
ADP
0.11 - 1055
ATP
0.18 - 294
Butyrate
0.37 - 1029
propionate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9 - 180
ATP
0.2 - 148
CTP
1.2 - 80
GTP
1 - 158
ITP
0.2 - 202
TTP
0.2 - 152
UTP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9
acetate
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pH 5.5, temperature not specified in the publication; pH and temperature not specified in the publication
0.0184 - 18.4
ADP
0.95 - 3.4
AlCl3
0.95 - 3.4
MgCl2
3
NaF
-
pH and temperature not specified in the publication
0.24
adenosine 5'-(gamma-thio)triphosphate
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pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.28
-
mutant D148A
3.4
-
mutant E384A
539
-
mutant N211A
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 hide
LITERATURE
7 - 7.4
-
acetate kinase activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
-
pH 6.0: about 75% of maximal activity, pH 8.5: about 65% of maximal activity, acetate kinase activity
5.5 - 9
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about 35% of maximum activity at pH 5.5 and 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
ACKA_METTE
408
0
44337
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
-
2 * 53000, denaturing gel electrophoresis
87000
-
non-denaturing, gradient gel electrophoresis
94000
-
gel filtration
53000
-
2 * 53000, alpha2 homodimer
94000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 53000, denaturing gel electrophoresis
dimer
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
three-dimensional structure of Methanosarcina thermophila acetate kinase bound to ADP
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in presence of substrate and transition states analogues
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space group C2, unit cell dimensions a = 181 A, b = 67 A, c = 83 A, beta 103 degrees
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
Q43W
-
site-directed mutagenesis, single mutant
R241A/Q43W
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site-directed mutagenesis, double mutant
R241K/Q43W
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site-directed mutagenesis, double mutant
R91A/Q43W
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site-directed mutagenesis, double mutant
R91K/Q43W
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site-directed mutagenesis, double mutant
D148A
-
site-directed mutagenesis
D148E
-
site-directed mutagenesis
D148N
-
site-directed mutagenesis
E384A
-
site-directed mutagenesis
E384D
-
site-directed mutagenesis
E384Q
-
site-directed mutagenesis
E97D
-
reduction of both Km and kcat-value
F179A
-
reduced catalytic efficiency with all substrates tested
H123A
-
site-directed mutagenesis
H152A
-
site-directed mutagenesis
H180A
-
site-directed mutagenesis
H180R
-
site-directed mutagenesis
H184A
-
site-directed mutagenesis
H208A
-
site-directed mutagenesis
H60A
-
site-directed mutagenesis
H90A
-
site-directed mutagenesis
H94A
-
site-directed mutagenesis
K14A
-
site-directed mutagenesis
K14R
-
site-directed mutagenesis
L122A
-
reduced catalytic efficiency with all substrates tested
N211A
-
site-directed mutagenesis
N7A
-
site-directed mutagenesis
P232A
-
reduced catalytic efficiency with all substrates tested
R175K
-
site-directed mutagenesis
R241A
-
severe decrease in kinetic parameters
R241L
-
severe decrease in kinetic parameters
R285A
-
site-directed mutagenesis
R285K
-
site-directed mutagenesis
R285L
-
site-directed mutagenesis
R340K
-
site-directed mutagenesis
R340L
-
site-directed mutagenesis
R91A
-
severe decrease in kinetic parameters
R91L
-
severe decrease in kinetic parameters
S10A
-
site-directed mutagenesis
S11A
-
site-directed mutagenesis
S12A
-
site-directed mutagenesis
V93A
-
improved catalytic efficiency with propionate and butyrate
V93G
-
improved catalytic efficiency with propionate and butyrate
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
the enzyme is unaffected by repeated freezing and thawing
-
all 4 substrates of the forward and reverse reaction protect the enzyme from inactivation by diethyldicarbonate
-
unaffected by repeated freezing and thawing
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is stable to oxygen
-
727804
stable to O2
-
642184
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen in liquid nitrogen, the enzyme is stable for at least months
-
-196°C, stable for at least 4 months in liquid nitrogen
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
judged by SDS-PAGE
-
purified wild-type and recombinant enzymes, R175L and R340A are unstable and cannot be purified
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
overexpressed in Escherichia coli BL21(DE3)
-
recombinant acetate kinase with a 6-residue N-terminal histidine tag is heterologously produced in Escherichia coli BL21(DE3)
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cloned and hyper-expressed in Escherichia coli
-
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 hide
LITERATURE
synthesis
-
protocol for overproduction of enzyme
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Methanosarcina thermophila (P38502)
Manually annotated by BRENDA team
Iyer, P.; Ferry, J.G.
Acetate kinase from Methanosarcina thermophila, a key enzyme for methanogenesis
Methods Biotechnol.
17
239-246
2005
Methanosarcina thermophila
-
Manually annotated by BRENDA team
Ingram-Smith, C.; Martin, S.R.; Smith, K.S.
Acetate kinase: not just a bacterial enzyme
Trends Microbiol.
14
249-253
2006
Aspergillus fumigatus, Aspergillus nidulans, Bacillus subtilis, Borreliella burgdorferi, Chaetomium globosum, Chlamydomonas reinhardtii, Coccidioides immitis, Coprinopsis cinerea, Cryptococcus neoformans, Cupriavidus necator, Entamoeba histolytica, Enterococcus faecalis, Fusarium graminearum, Helicobacter pylori, Histoplasma capsulatum, Lactobacillus acidophilus, Lactococcus lactis, Listeria monocytogenes, Magnaporthe grisea, Mesoplasma florum, Methanosarcina acetivorans, Methanosarcina mazei, Methanosarcina thermophila, Mycoplasma pneumoniae, Neurospora crassa, Oceanobacillus iheyensis, Parastagonospora nodorum, Phanerochaete chrysosporium, Phytophthora ramorum, Phytophthora sojae, Salmonella enterica, Sclerotinia sclerotiorum, Staphylococcus aureus, Streptococcus pneumoniae, Trichoderma reesei, Uncinocarpus reesii, Ustilago maydis
Manually annotated by BRENDA team
Gorrell, A.; Ferry, J.G.
Investigation of the Methanosarcina thermophila acetate kinase mechanism by fluorescence quenching
Biochemistry
46
14170-14176
2007
Methanosarcina thermophila, Methanosarcina thermophila (P38502)
Manually annotated by BRENDA team
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, Methanosarcina thermophila (P38502)
Manually annotated by BRENDA team
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, Methanosarcina thermophila (P38502), Methanosarcina thermophila TM-1 (P38502)
Manually annotated by BRENDA team
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, Methanosarcina thermophila (P38502)
Manually annotated by BRENDA team
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, Methanosarcina thermophila (P38502)
Manually annotated by BRENDA team
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