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Information on EC 4.2.1.1 - carbonic anhydrase and Organism(s) Methanosarcina thermophila and UniProt Accession P40881

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.1 carbonic anhydrase
IUBMB Comments
The enzyme catalyses the reversible hydration of gaseous CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH. It is widespread and found in archaea, bacteria, and eukaryotes. Three distinct classes exist, and appear to have evolved independently. Contains zinc.
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This record set is specific for:
Methanosarcina thermophila
UNIPROT: P40881
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Word Map
The taxonomic range for the selected organisms is: Methanosarcina thermophila
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
carbonic anhydrase, ca ix, ca ii, hca ii, hca i, carbonic anhydrase ix, carbonic anhydrase ii, hca ix, ca iv, anhydrase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
gamma-class carbonic anhydrase
-
anhydrase
-
-
-
-
CA
-
-
-
-
CA-IX
-
-
-
-
CA-VA
-
-
-
-
CA-VB
-
-
-
-
CA-VI
-
-
-
-
CA-VII
-
-
-
-
CA-XII
-
-
-
-
CA-XIV
-
-
-
-
CA1
-
-
-
-
CA2
-
-
-
-
CAIX
-
-
-
-
carbonate anhydrase
-
-
-
-
Carbonate dehydratase
-
-
-
-
Carbonate dehydratase IX
-
-
-
-
Carbonate dehydratase VA
-
-
-
-
Carbonate dehydratase VB
-
-
-
-
Carbonate dehydratase VI
-
-
-
-
Carbonate dehydratase VII
-
-
-
-
Carbonate dehydratase XII
-
-
-
-
Carbonate dehydratase XIV
-
-
-
-
carbonic acid anhydrase
-
-
-
-
carbonic anhydrase
carbonic anhydrase cambialistic enzyme
-
-
carbonic dehydratase
-
-
-
-
carboxyanhydrase
-
-
-
-
dehydratase, carbonate
-
-
-
-
gamma-carbonic anhydrase
-
-
gamma-class carbonic anhydrase
-
-
Membrane antigen MN
-
-
-
-
P54/58N
-
-
-
-
pMW1
-
-
-
-
RCC-associated antigen G250
-
-
-
-
Renal cell carcinoma-associated antigen G250
-
-
-
-
Salivary carbonic anhydrase
-
-
-
-
Secreted carbonic anhydrase
-
-
-
-
Tumor antigen HOM-RCC-3.1.3
-
-
-
-
additional information
-
the enzyme from Methanosorcina thermophila belongs to the gamma class carbonic anhydrases
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
H2CO3 = CO2 + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
addition
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
carbonic acid hydro-lyase (carbon-dioxide-forming)
The enzyme catalyses the reversible hydration of gaseous CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH. It is widespread and found in archaea, bacteria, and eukaryotes. Three distinct classes exist, and appear to have evolved independently. Contains zinc.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-03-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CO2 + H2O
H2CO3
show the reaction diagram
H2CO3
CO2 + H2O
show the reaction diagram
CO2 + H2O
H2CO3
show the reaction diagram
H2CO3
CO2 + H2O
show the reaction diagram
additional information
?
-
-
no esterase activity
-
-
?
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
H2CO3
CO2 + H2O
show the reaction diagram
H2CO3
CO2 + H2O
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
can substitute for Zn2+
Fe2+
anaerobic reconstitution of apoenzyme with Fe2+, which yields an enzyme with an effective kcat that exceeds that for the Zn2+-reconstituted enzyme. The Fe2+-reconstituted enzyme contains high spin Fe2+ that, when oxidized to Fe3+, inactivates the enzyme. Reconstitution with Fe3+ is unsuccessful
Cd2+
-
replacement of zinc ion with cadmium does not entail significant differences in the catalytic performance of the enzyme
Zinc
-
contains 1 Zn per subunit
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,5-bis[amino(dihydroxy)-lambda4-sulfanyl]-2,3-dichlorobenzene
-
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]ethanamine
-
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]methanamine
-
2,4-bis[amino(dihydroxy)-lamba4-sulfanyl]-5-(trifluoromethyl)aniline
-
2,4-bis[amino(dihydroxy)-lambda4-sulfanyl]-5-chloroaniline
-
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme gammaCA
3-[amino(dihydroxy)-lambda4-sulfanyl]aniline
-
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme gammaCA, i.e. daranide
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
-
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-bromoaniline
-
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-chloroaniline
-
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-fluoroaniline
-
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-iodoaniline
-
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme gammaCA
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme gammaCA
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme gammaCA
acetazolamide
CN-
best anion inhibitors for Zn2+-substituted enzyme are cyanate and hydrogen sulfide
Cyanate
IC50: 0.28 mM
cyanide
IC50: 0.31 mM
ethoxzolamide
HS-
best anion inhibitors for Zn2+-substituted enzyme are cyanate and hydrogen sulfide
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme gammaCA
sulfanilamide
topiramate
[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]hydrazine
-
acetazolamide
-
-
azide
weak inhibitor of the Zn(II)-substituted enzyme
Carbonate
weak inhibitor of the Zn(II)-substituted enzyme, best inhibitor of the Co(II)-substituted enzyme
Cyanate
best inhibitor of the Zn(II)-substituted enzyme
hydrogen sulfide
best inhibitor of the Zn(II)-substituted enzyme
hydrogen sulfite
weak inhibitor of the Zn(II)-substituted enzyme
hydrogencarbonate
good inhibitor of the Co(II)-substituted enzyme
nitrate
good inhibitor of the Co(II)-substituted enzyme
nitrite
weak inhibitor of the Zn(II)-substituted enzyme
sulfanilamide
-
-
thiocyanate
weak inhibitor of the Zn(II)-substituted enzyme
Zn2+
-
the enzyme binds three catalytic Zn2+ ions at symmetry-related subunit interfaces. Zinc binding drives the folding and association of the homotrimeric enzyme
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(2-aminoethyl)-piperazine
-
effectively activates Zn-gamma-class carbonic anhydrase
2-pyridyl-methylamine
-
-
2-pyridylmethylamine
-
effectively activates Zn-gamma-class carbonic anhydrase
4-(2-aminoethyl)-morpholine
-
-
4-amino-L-phenylalanine
-
-
air
the enzyme loses activity when it was exposed to air
-
D-3,4-dihydroxyphenylalanine
-
-
H2O2
the enzyme loses activity when it was exposed to 3% H2O2
imidazole
addition of 50 mM imidazole to the assay buffer increases the kcat of the enzyme more than 4fold
L-3,4-dihydroxyphenylalanine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.09 - 51.4
CO2
0.8 - 44.1
CO2
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 120100
CO2
0.000493 - 71900
CO2
68000 - 243000
H2CO3
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
400 - 10300
CO2
0.00016 - 0.0017
CO2
3100 - 5400
H2CO3
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00015 - 0.00019
1,5-bis[amino(dihydroxy)-lambda4-sulfanyl]-2,3-dichlorobenzene
0.00027 - 0.0013
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]ethanamine
0.00035 - 0.0085
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]methanamine
0.00083 - 0.00095
2,4-bis[amino(dihydroxy)-lamba4-sulfanyl]-5-(trifluoromethyl)aniline
0.00012 - 0.00061
2,4-bis[amino(dihydroxy)-lambda4-sulfanyl]-5-chloroaniline
0.00046
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme gammaCA
0.00017 - 0.00124
3-[amino(dihydroxy)-lambda4-sulfanyl]aniline
0.00019
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme gammaCA, i.e. daranide
0.00018 - 0.00636
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
0.00028 - 0.00172
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-bromoaniline
0.00014 - 0.00074
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-chloroaniline
0.00097 - 0.0042
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-fluoroaniline
0.00028 - 0.00066
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-iodoaniline
0.00012
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme gammaCA
0.00041
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme gammaCA
0.00083
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme gammaCA
0.000063 - 0.00143
acetazolamide
22.2 - 160
Br-
0.00014 - 0.00101
celecoxib
0.68 - 51.5
CN-
0.09 - 4.7
CNO-
0.009 - 6.7
CO32-
0.00041 - 0.00171
dorzolamide
0.0002 - 0.00074
ethoxzolamide
0.1 - 42
HCO3-
0.05 - 2
HS-
1.8 - 11.7
HSO3-
5.3 - 160
I-
0.00014 - 0.00017
methazolamide
0.00014
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme gammaCA
4.9 - 5.8
N3-
6.8 - 7.3
NO2-
0.09 - 36.5
NO3-
6.1 - 7
SCN-
0.000096 - 0.00336
sulfamic acid
0.00596 - 0.069
sulfamide
0.00025 - 0.00393
sulfanilamide
0.00012 - 0.00102
topiramate
0.00013 - 0.00024
valdecoxib
0.00022 - 0.0022
[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]hydrazine
4.9 - 5.8
azide
22.2 - 160
Br-
0.009 - 6.7
Carbonate
0.09 - 4.7
Cyanate
0.68 - 51.5
cyanide
0.05 - 2
hydrogen sulfide
1.8 - 11.7
hydrogen sulfite
0.1 - 42
hydrogencarbonate
5.3 - 160
I-
0.09 - 36.5
nitrate
6.8 - 7.3
nitrite
6.1 - 7
thiocyanate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
acetazolamide
Methanosarcina thermophila
IC50: 0.4 mM
3.4
azide
Methanosarcina thermophila
IC50: 3.4 mM
0.28
Cyanate
Methanosarcina thermophila
IC50: 0.28 mM
0.31
cyanide
Methanosarcina thermophila
IC50: 0.31 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
15 min, stable
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
calculation from nucleotide sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
Manually annotated by BRENDA team
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
Manually annotated by BRENDA team
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
carbonic anhydrase represents one of the most ancient proteins
physiological function
-
gamma-CAs are widely distributed in all three phylogenetic domains of life, playing important roles in the global carbon cycle
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22873
3 * 22873, measuring A280 value of protein solution
22900
4 * 22900, calculation from nucleotide sequence
20000
2 * 20000, SDS-PAGE
22873
-
3 * 22873, determined by measuring A280S of protein solution
22900
70000
74000
84000
-
authentic enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 22900, calculation from nucleotide sequence
trimer
3 * 22873, measuring A280 value of protein solution
heterotrimer
2 * 20000, SDS-PAGE
tetramer
-
or trimer, 3 * or 4 * 22900, calculation from nucleotide sequence
trimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
the discrepancy in molecular weight between the recombinant and the authentic enzyme suggests that the carbonic anhydrase is posttranslationally modified in either E. coli or Methanobacterium thermophilum
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cubic crystals, space group P2(1)3, Zn-Cam, unit cell a : b : c: 82.64 A, Zn-Cam-HCO3-, unit cell a : b : c: 82.51 A, Zn-Cam-SO42-, unit cell a : b : c: 82.68 A, Co-Cam, unit cell a : b : c: 82.34 A, Co-Cam-HCO3-, unit cell a : b : c: 82.58 A, Co-Cam-SO42-, unit cell a : b : c: 82.61 A
hanging-drop vapor diffusion technique
the crystal structure of the enzyme is determined at 2.8 A resolution using the method of multiple isomorphous replacement in combination with 3fold non-crystallographic symmetry averaging and phase extension
purified enzyme in complex with Zn2+ and Co2+, X-ray diffraction structure determination and analysis, PDB ID 1QRG
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R59A
site-directed mutagenesis
R59C
site-directed mutagenesis
R59E
site-directed mutagenesis
R59H
site-directed mutagenesis
R59K
site-directed mutagenesis
R59M
site-directed mutagenesis
R59Q
site-directed mutagenesis
W19A
kcat/km at pH 7.5 is 2.5fold lower than wild-type value, kcat/km at pH 8.8 is 2.2fold lower than wild-type value
W19F
kcat/km at pH 7.5 is 5fold lower than wild-type value, kcat/km at pH 8.8 is 5.2fold lower than wild-type value
W19N
kcat/km at pH 7.5 is 3.2fold lower than wild-type value, kcat/km at pH 8.8 is 2.4fold lower than wild-type value
Y200A
kcat/km at pH 7.5 is 3.5fold higher than wild-type value, kcat/km at pH 8.8 is 3.3fold higher than wild-type value
Y200F
kcat/km at pH 7.5 is 3.6fold higher than wild-type value, kcat/km at pH 8.8 is 2.5fold lower than wild-type value
Y200S
kcat/km at pH 7.5 is 3fold higher than wild-type value, kcat/km at pH 8.8 is 3.3fold higher than wild-type value
C148S
-
the mutation eliminate potential problems with the oxidation of the single cysteine residue at position 148
E62A
-
site-directed mutagenesis, large decrease in kcat
E62A/E84A
-
site-directed mutagenesis, large decrease in kcat
E62C
-
site-directed mutagenesis, large decrease in kcat
E62D
-
site-directed mutagenesis, 3fold decrease in kcat
E62D/E84D
-
site-directed mutagenesis, large decrease in kcat
E62H
-
site-directed mutagenesis, large decrease in kcat
E62Q
-
site-directed mutagenesis, large decrease in kcat
E62T
-
site-directed mutagenesis, large decrease in kcat
E62Y
-
site-directed mutagenesis, large decrease in kcat
E84 A
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 C
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 D
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 H
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 K
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 Q
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 S
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 Y
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84A
-
proton shuttle replaced with a residue that does not transfer protons
E88A
-
site-directed mutagenesis, large decrease in kcat
E89A
-
site-directed mutagenesis, large decrease in kcat
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 75
-
the purified enzyme retains catalytic activity if incubated for 15 min at 55°C, but only a little activity is recovered when the enzyme is incubated above 75°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing results in formation of aggregates, unfolded at 1.5 M guanidine hydrochloride
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme loses activity when it is exposed to air or 3% H2O2
727748
the enzyme produced in vivo is sensitive to oxygen, losing 90% of activity in 5 min after exposure to air
-
696355
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the recombinant enzyme is purified anaerobically
recombinant enzyme from Escherichia coli anaerobically or aerobically, recombinant enzyme from Methanosarcina acetivorans anaerobically
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
produced in Escherichia coli
wild-type and variants expressed in Escherichia coli BL21(DE3) or BL21(DE3) Gold
cam gene expressed in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli and Methanosarcina acetivorans
-
expressed in Escherichia coli BL21(DE3) or Bl21(DE3) Gold
-
expression in Escherichia coli
-
overexpression in Escherichia coli
-
overproduced in Escherichia coli
recombinant enzyme expression in Escherichia coli or in Methanosarcina acetivorans
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
-
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Alber, B.E.; Ferry, J.G.
Characterization of heterologously produced carbonic anhydrase from Methanosarcina thermophila
J. Bacteriol.
178
3270-3274
1996
Methanosarcina thermophila
Manually annotated by BRENDA team
Alber, B.E.; Colangelo, C.M.; Dong, J.; Stalhandske, C.M.V.; Baird, T.T.; Tu, C.; Fierke, C.A.; Silverman, D.N.; Scott, R.A.; Ferry, J.G.
Kinetic and spectroscopic characterization of the gamma-carbonic anhydrase from the methanoarcheon Methanosarcina thermophila
Biochemistry
38
13119-13128
1999
Methanosarcina thermophila
Manually annotated by BRENDA team
Iverson, T.M.; Alber, B.E.; Kisker, C.; Ferry, J.G.; Rees, D.C.
A closer look at the active site of gamma-class carbonic anhydrases: High resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila
Biochemistry
39
9222-9231
2000
Methanosarcina thermophila (P40881), Methanosarcina thermophila
Manually annotated by BRENDA team
Tripp, B.C.; Ferry, J.G.
A structure-function study of a proton transport pathway in teh gamma-class carbonic anhydrase from Methanosarcina thermophila
Biochemistry
39
9232-9240
2000
Methanosarcina thermophila
Manually annotated by BRENDA team
Tu, C.; Rowlett, R.S.; Tripp, B.C.; Ferry, J.G.; Silverman, D.N.
Chemical rescue of proton transfer in catalysis by carbonic anhydrases in the beta- and gamma-class
Biochemistry
41
15429-15435
2002
Arabidopsis thaliana, Methanosarcina thermophila
Manually annotated by BRENDA team
Tripp, B.C.; Tu, C.; Ferry, J.G.
Role of the arginine 59 in the gamma-class carbonic anhydrases
Biochemistry
41
669-678
2002
Methanosarcina thermophila (P40881)
Manually annotated by BRENDA team
Tu, C.; Tripp, B.C.; Ferry, J.G.; Silverman, D.N.
Bicarbonate as a proton donor in catalysis by Zn(II)- and Co(II)-containing carbonic anhydrases
J. Am. Chem. Soc.
123
5861-5866
2001
Homo sapiens, Methanosarcina thermophila
Manually annotated by BRENDA team
Alber, B.E.; Ferry, J.G.
A carbonic anhydrase from the archaeon Methanosarcina thermophila
Proc. Natl. Acad. Sci. USA
91
6909-6913
1994
Methanosarcina thermophila (P40881), Methanosarcina thermophila
Manually annotated by BRENDA team
Alterio, V.; De Simone, G.; Monti, S.M.; Scozzafava, A.; Supuran, C.T.
Carbonic anhydrase inhibitors: inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides - solution and crystallographic studies
Bioorg. Med. Chem. Lett.
17
4201-4207
2007
Helicobacter pylori (O24855), Helicobacter pylori (Q1CVF1), Homo sapiens (O43570), Homo sapiens (P00915), Homo sapiens (P00918), Homo sapiens (P07451), Homo sapiens (P22748), Homo sapiens (P23280), Homo sapiens (P35218), Homo sapiens (P43166), Homo sapiens (Q16790), Homo sapiens (Q9ULX7), Homo sapiens (Q9Y2D0), Homo sapiens, Methanosarcina thermophila (P40881), Mus musculus (Q9D6N1)
Manually annotated by BRENDA team
Macauley, S.R.; Zimmerman, S.A.; Apolinario, E.E.; Evilia, C.; Hou, Y.M.; Ferry, J.G.; Sowers, K.R.
The archetype gamma-class carbonic anhydrase (Cam) contains iron when synthesized in vivo
Biochemistry
48
817-819
2009
Methanosarcina thermophila
Manually annotated by BRENDA team
Innocenti, A.; Zimmerman, S.A.; Scozzafava, A.; Ferry, J.G.; Supuran, C.T.
Carbonic anhydrase activators: activation of the archaeal beta-class (Cab) and gamma-class (Cam) carbonic anhydrases with amino acids and amines
Bioorg. Med. Chem. Lett.
18
6194-6198
2008
Methanothermobacter thermautotrophicus, Methanosarcina thermophila
Manually annotated by BRENDA team
Amata, O.; Marino, T.; Russo, N.; Toscano, M.
Catalytic activity of a zeta-class zinc and cadmium containing carbonic anhydrase. Compared work mechanisms
Phys. Chem. Chem. Phys.
13
3468-3477
2011
Methanosarcina thermophila, Conticribra weissflogii
Manually annotated by BRENDA team
Zimmerman, S.; Domsic, J.F.; Tu, C.; Robbins, A.H.; McKenna, R.; Silverman, D.N.; Ferry, J.G.
Role of Trp19 and Tyr200 in catalysis by the gamma-class carbonic anhydrase from Methanosarcina thermophila
Arch. Biochem. Biophys.
529
11-17
2013
Methanosarcina thermophila (P40881), Methanosarcina thermophila
Manually annotated by BRENDA team
Innocenti, A.; Zimmerman. S.; Ferry, J.G.; Scozzafava, A.; Supuran, C.T.
Carbonic anhydrase inhibitors. Inhibition of the zinc and cobalt gamma-class enzyme from the archaeon Methanosarcina thermophila with anions
Bioorg. Med. Chem. Lett.
14
3327-3331
2004
Methanosarcina thermophila, Methanosarcina thermophila (P40881)
Manually annotated by BRENDA team
Zimmerman, S.; Innocenti, A.; Casini, A.; Ferry, J.G.; Scozzafava, A.; Supuran, C.T.
Carbonic anhydrase inhibitors. Inhibition of the prokariotic beta and gamma-class enzymes from Archaea with sulfonamides
Bioorg. Med. Chem. Lett.
14
6001-6006
2004
Methanothermobacter thermautotrophicus, Methanosarcina thermophila (P40881), Methanosarcina thermophila
Manually annotated by BRENDA team
Kisker, C.; Schindelin, H.; Alber, B.E.; Ferry, J.G.; Rees, D.C.
A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila
EMBO J.
15
2323-2330
1996
Methanosarcina thermophila (P40881), Methanosarcina thermophila
Manually annotated by BRENDA team
Zimmerman, S.A.; Tomb, J.F.; Ferry, J.G.
Characterization of CamH from Methanosarcina thermophila, founding member of a subclass of the gamma class of carbonic anhydrases
J. Bacteriol.
192
1353-1360
2010
Methanosarcina thermophila (C3W4Q7), Methanosarcina thermophila TM-1 (C3W4Q7)
Manually annotated by BRENDA team
Tripp, B.C.; Bell, C.B.; Cruz, F.; Krebs, C.; Ferry, J.G.
A role for iron in an ancient carbonic anhydrase
J. Biol. Chem.
279
6683-6687
2004
Methanosarcina thermophila, Methanosarcina thermophila (P40881)
Manually annotated by BRENDA team
Simler, B.R.; Doyle, B.L.; Matthews, C.R.
Zinc binding drives the folding and association of the homo-trimeric gamma-carbonic anhydrase from Methanosarcina thermophila
Protein Eng. Des. Sel.
17
285-291
2004
Methanosarcina thermophila
Manually annotated by BRENDA team
Di Fiore, A.; Alterio, V.; Monti, S.M.; De Simone, G.; D'Ambrosio, K.
Thermostable carbonic anhydrases in biotechnological applications
Int. J. Mol. Sci.
16
15456-15480
2015
Methanosarcina thermophila, Sulfurihydrogenibium azorense, Citrobacter freundii (A0A0D7LLM5), Caminibacter mediatlanticus (A6DAW8), Sulfurihydrogenibium sp. YO3AOP1 (B2V8E3), Persephonella marina (C0QRB5), Methanothermobacter thermautotrophicus (D9PU79), Thermovibrio ammonificans (E8T502), Serratia sp. ISTD04 (K4N028), Pyrococcus horikoshii (O59257), Homo sapiens (P00918), Bos taurus (P00921), Desulfovibrio vulgaris (Q72B61), Caminibacter mediatlanticus TB-2 (A6DAW8), Desulfovibrio vulgaris Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303 (Q72B61), Persephonella marina DSM 14350 / EX-H1 (C0QRB5), Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg (D9PU79), Thermovibrio ammonificans DSM 15698 / JCM 12110 / HB-1 (E8T502)
Manually annotated by BRENDA team