Literature summary for 4.2.1.1 extracted from

Perfetto, R.; Del Prete, S.; Vullo, D.; Sansone, G.; Barone, C.; Rossi, M.; Supuran, C.T.; Capasso, C.
Biochemical characterization of the native alpha-carbonic anhydrase purified from the mantle of the Mediterranean mussel, Mytilus galloprovincialis (2017), J. Enzyme Inhib. Med. Chem., 32, 632-639 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
acetazolamide	-	Mytilus galloprovincialis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	stopped-flow technique, kinetic analysis	Mytilus galloprovincialis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytoplasm	-	Mytilus galloprovincialis	5737	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the metalloenzyme, the Zn(II) ion is crucial for catalysis, the enzyme sequence contains the three His residues acting as zinc ligands	Mytilus galloprovincialis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
50000	-	native enzyme, native PAGE	Mytilus galloprovincialis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
H2CO3	Mytilus galloprovincialis	-	CO2 + H2O	-	r

Organism

Organism	UniProt	Comment	Textmining
Mytilus galloprovincialis	A0A0N9FGL8	-	-

Purification (Commentary)

Purification (Comment)	Organism
native soluble enzyme from mantle by ammonium sulfate fractionation, anion exchange chromatography, and pAMBS affinity chromatography, to homogeneity	Mytilus galloprovincialis

Source Tissue

Source Tissue	Comment	Organism	Textmining
mantle	-	Mytilus galloprovincialis	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
H2CO3	-	Mytilus galloprovincialis	CO2 + H2O	-	r
additional information	4-nitrophenylacetate is used as activity assay substrate	Mytilus galloprovincialis	?	-	?

Subunits

Subunits	Comment	Organism
monomer or dimer	x * 50000, native enzyme, SDS-PAGE, x * 26000, about, sequence calculation	Mytilus galloprovincialis
More	primary structure analysis	Mytilus galloprovincialis

Synonyms

Synonyms	Comment	Organism
alpha-CA	-	Mytilus galloprovincialis
alpha-carbonic anhydrase	-	Mytilus galloprovincialis
CAII	-	Mytilus galloprovincialis
carbonic anhydrase II	-	Mytilus galloprovincialis
MgaCA	-	Mytilus galloprovincialis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
22	-	assay at room temperature	Mytilus galloprovincialis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.3	-	assay at	Mytilus galloprovincialis

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.00038	-	acetazolamide	CO2 hydration, pH 8.3, 22°C, native enzyme	Mytilus galloprovincialis

General Information

General Information	Comment	Organism
additional information	the Mytilus galloprovincialis alpha-CA sequence contains the three His residues (His94, His96, and His119) acting as zinc ligands and the gate-keeper residues present in all alpha-CAs (Glu106 and Thr199), but has a Lys in position 64 and not a His as proton shuttling residue	Mytilus galloprovincialis
physiological function	the Mytilus galloprovincialis alpha-CA is involved in pH regulation and/or in the delivery of bicarbonate helping the mussel during the formation of the shell	Mytilus galloprovincialis

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Release 2023.1 (January 2023)