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Information on EC 4.2.1.1 - carbonic anhydrase and Organism(s) Spinacia oleracea and UniProt Accession P16016

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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:
Spinacia oleracea
UNIPROT: P16016
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The taxonomic range for the selected organisms is: Spinacia oleracea
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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H2CO3
=
CO2
+
H2O
=
+
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-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 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
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
H2CO3 = CO2 + H2O
show the reaction diagram
zinc-hydroxide mechanism, rate-determining H+ transfer step in catalytic mechanism
-
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
-
-
r
CO2 + H2O
H2CO3
show the reaction diagram
H2CO3
CO2 + H2O
show the reaction diagram
-
-
-
r
additional information
?
-
-
CO2/HCO3- exchange
-
-
?
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
Zn2+
zinc hydroxide mechanism
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-acetamido-1,3,4-thiadiazole-2-sulfonamide
-
-
ethylsulfonamide
-
-
methylsulfonamide
-
-
n-hexylsulfonamide
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
influence of buffer composition and pH on the turnover-number
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
spinach
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CAHC_SPIOL
319
0
34570
Swiss-Prot
Chloroplast (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
212000
-
gel filtration
26000
-
8 * 26000, SDS-PAGE
30000
-
6 * 30000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
6 * 30000, SDS-PAGE
octamer
-
8 * 26000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
most thermostable carbonic anhydrase, retains 90% activity after incubation for 15 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-14°C, enzyme as a suspension in saturated (NH4)2SO4 containing 0.02 M sodium phosphate buffer, 0.1 M NaCl and 0.001 M EDTA, pH 6.8, stable for 2 months
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
carbonic anhydrase assay based on membrane inlet mass spectrometry. A quantitative assessment of the carbonic anhydrase activity in photosystem II
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pocker, Y.; Miksch, R.R.
Plant carbonic anhydrase. Properties and bicarbonate dehydration kinetics
Biochemistry
17
1119-1125
1978
Spinacia oleracea
Manually annotated by BRENDA team
Kandel, M.; Gornall, A.G.; Cybulsky, D.L.; Kandel, S.I.
Carbonic anhydrase from spinach leaves. Isolation and some chemical properties
J. Biol. Chem.
253
679-685
1978
Spinacia oleracea
Manually annotated by BRENDA team
Pocker, Y.; Ng, J.S.Y.
Plant carbonic anhydrase. Properties and carbon dioxide hydration kinetics
Biochemistry
12
5127-5134
1973
Spinacia oleracea
Manually annotated by BRENDA team
Rowlett, R.S.; Chance, M.R.; Wirt, M.D.; Sidelinger, D.E.; Royal, J.R.; Woodroffe, M.; Wang, Y.F.A.; Saha, R.P.; Lam, M.G.
Kinetic and structural characterization of spinach carbonic anhydrase
Biochemistry
33
13967-13976
1994
Spinacia oleracea
Manually annotated by BRENDA team
Smith, K.S.; Cosper, N.J.; Stalhandske, C.; Scott, R.A.; Ferry, J.G.
Structural and kinetic characterization of an archaeal beta-class carbonic anhydrase
J. Bacteriol.
182
6605-6613
2000
Spinacia oleracea (P16016), Spinacia oleracea, Methanothermobacter thermautotrophicus (Q50565), Methanothermobacter thermautotrophicus
Manually annotated by BRENDA team
McConnell, I.L.; Badger, M.R.; Wydrzynski, T.; Hillier, W.
A quantitative assessment of the carbonic anhydrase activity in photosystem II
Biochim. Biophys. Acta
1767
639-647
2007
Spinacia oleracea
Manually annotated by BRENDA team