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Information on EC 4.2.1.1 - carbonic anhydrase and Organism(s) Neisseria gonorrhoeae and UniProt Accession Q50940

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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:
Neisseria gonorrhoeae
UNIPROT: Q50940
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Word Map
The taxonomic range for the selected organisms is: Neisseria gonorrhoeae
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
anhydrase
-
-
-
-
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 dehydratase
-
-
-
-
carboxyanhydrase
-
-
-
-
dehydratase, carbonate
-
-
-
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
addition
-
-
-
-
dehydration
-
-
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
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
?
CO2 + H2O
H2CO3
show the reaction diagram
H2CO3
CO2 + H2O
show the reaction diagram
-
-
-
r
additional information
?
-
-
esterase activity with p-nitrophenyl acetate
-
-
?
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
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
can substitute for Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-ethoxy-2-benzo-thiazolesulfonamide
-
-
CN-
-
anion inhibition of the esterase activity
guanidine hydrochloride
-
-
N3-
-
anion inhibition of the esterase activity
NCO-
-
anion inhibition of the esterase activity
SCN-
-
anion inhibition of the esterase activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3133
CO2
-
purified recombinant enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000025 - 0.000084
6-ethoxy-2-benzo-thiazolesulfonamide
0.092
CN-
-
pH 6.7, 25°C
0.56
N3-
-
pH 6.7, 25°C
0.027
NCO-
-
pH 6.7, 25°C
1.16
SCN-
-
pH 6.7, 25°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CAH_NEIGO
252
0
28085
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
SDS-PAGE
28000
-
x * 28000, SDS-PAGE
28085
-
x * 28085, a 26-residue signal peptide is cleaved off by the Escherichia coli processing machinery, thus the recombinant enzyme has a MW of 26314 Da, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
a 26-residue signal peptide is cleaved off by the E. coli processing machinery
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complex with the inhibitor acetazolamide
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H66A
-
higher sensitivity to inhibitor 6-ethoxy-2-benzo-thiazolesulfonamide
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
guanidine hydrochloride causes denaturation and inactivation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and expressed in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
-
overexpression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chirica, L.C.; Elleby, B.; Jonsson, B.H.; Lindskog, S.
The complete sequence, expression in Escherichia coli, purification and some properties of carbonic anhydrase from Neisseria gonorrhoeae
Eur. J. Biochem.
244
755-760
1997
Neisseria gonorrhoeae
Manually annotated by BRENDA team
Huang, S.; Xue, Y.; Sauer-Eriksson, E.; Chirica, L.; Lindskog, S.; Jonsson, B.H.
Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetazolamide
J. Mol. Biol.
283
301-310
1998
Neisseria gonorrhoeae (Q50940), Neisseria gonorrhoeae
Manually annotated by BRENDA team
Elleby, B.; Chirica, L.C.; Tu, C.; Zeppezauer, M.; Lindskog, S.
Characterization of carbonic anhydrase from Neisseria gonorrhoeae
Eur. J. Biochem.
268
1613-1619
2001
Neisseria gonorrhoeae
Manually annotated by BRENDA team
Liu, Z.; Bartlow, P.; Dilmore, R.M.; Soong, Y.; Pan, Z.; Koepsel, R.; Ataai, M.
Production, purification, and characterization of a fusion protein of carbonic anhydrase from Neisseria gonorrhoeae and cellulose binding domain from Clostridium thermocellum
Biotechnol. Prog.
25
68-74
2009
Neisseria gonorrhoeae
Manually annotated by BRENDA team