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Information on EC 4.2.1.1 - carbonic anhydrase and Organism(s) Haemophilus influenzae and UniProt Accession P45148

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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:
Haemophilus influenzae
UNIPROT: P45148
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Word Map
The taxonomic range for the selected organisms is: Haemophilus influenzae
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
beta-carbonic anhydrase
-
anhydrase
-
-
-
-
beta-carbonic 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
-
-
-
-
carbonate hydrolyase
-
-
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
-
-
-
-
additional information
HICA is a type II member of the beta-carbonic anhydrase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
H2CO3 = CO2 + H2O
show the reaction diagram
reaction mechanism, overview
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
H2CO3
CO2 + H2O
show the reaction diagram
H2CO3
CO2 + H2O
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
H2CO3
CO2 + H2O
show the reaction diagram
-
-
-
r
H2CO3
CO2 + H2O
show the reaction diagram
-
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfate
the sulfate ion competes with the bicarbonate ion for the binding site near the active site affecting the allosteric regulation of the enzyme, binding structure in wild-type an dmutant enzymes, overview
Zn2+
a zinc-metalloenzyme
Co2+
-
preparation of a Co(II)-substituted HICA, Co-HICA. Co(II)-substituted HICA, Co-HICA, has comparable, 20% enhanced kcat and 2.3fold increased Km/kcat compared to that of the wild-type enzyme
Zn2+
-
required, can be substituted by Co2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bicarbonate
-
is hypothesized to be an allosteric inhibitor of HICA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10.5
-
pH profile, pH-dependent changes in the absorption spectrum of Co-HICA including an increase in molar absorptivity and a red shift of a 580 nm peak with decreasing pH, correlate with the pH-dependence of kcat/Km, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
HICA is a type II member of the beta-carbonic anhydrase family
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
about, recombinant Co-HICA, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
recombinant Co-HICA, the crystal structure shows a four-coordinate geometry for Co-HICA with pH-dependent changes in the absorption spectrum of Co-HICA, overview
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified wild-type and mutant enzymes, 12 mg/ml protein mixed with 0.7 M sodium potassium tartrate, 0.10 M HEPES, pH 7.5, for tetragonal crystals and with 1.8 M ammonium sulfate, 4% PEG 400, 0.10 M HEPES, pH 7.5, for monoclinic crystals, 22°C, 2-3 days, crystals are soaked for 1-2 min in artificial mother liquor plus either 30% glucose or 30% glucose and 100 mM NaHCO3, X-ray diffraction structure determination and analysis
purified recombinant Co-HICA by hanging drop vapor diffusion, 10 mg/ml protein crystallized in 0.2 M sodium acetate, 0.1 M Tris-HCl, pH 8.5, 0.1 M (NH4)2SO4, and 27% PEG 4000, 22°C, several days, X-ray diffraction structure determination and analysis at 2.5 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G41A
the mutant has kcat/Km values similar to wild-type enzyme, and exhibits a similar dramatic decrease in catalytic activity at pH values below pH 8.0, but HICA-G41A is serendipitously found to bind sulfate ion or bicarbonate ion near pairs of Glu50 and Arg64 residues located on the dimerization interface, 2 of 12 chains in the asymmetric unit bind bicarbonate ion exclusively at the dimerization interface, while the remaining 10 chains bind bicarbonate ion exclusively at the allosteric site
V47A
the mutant has kcat/Km values similar to wild-type enzyme, and exhibits a similar dramatic decrease in catalytic activity at pH values below pH 8.0, but HICA-V47A is serendipitously found to bind sulfate ion or bicarbonate ion near pairs of Glu50 and Arg64 residues located on the dimerization interface, bicarbonate ions simultaneously bind to both the dimerization interface and the allosteric sites
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant mutants V47A and G41A to homogeneity from Escherichia coli by ion exchange and hydrophobic interaction chromatography, and gel filtration
recombinant Co-HICA from Escherichia coli by gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of wild-type enzyme and mutants V47A and G41A in Escherichia coli
overexpression of HICA in Escherichia coli in minimal media supplemented with CoCl2
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hoffmann, K.M.; Samardzic, D.; Heever, K.; Rowlett, R.S.
Co(II)-substituted Haemophilus influenzae beta-carbonic anhydrase: spectral evidence for allosteric regulation by pH and bicarbonate ion
Arch. Biochem. Biophys.
511
80-87
2011
Haemophilus influenzae
Manually annotated by BRENDA team
Rowlett, R.S.; Hoffmann, K.M.; Failing, H.; Mysliwiec, M.M.; Samardzic, D.
Evidence for a bicarbonate escort site in Haemophilus influenzae beta-carbonic anhydrase
Biochemistry
49
3640-3647
2010
Haemophilus influenzae (P45148), Haemophilus influenzae
Manually annotated by BRENDA team