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Search results 1 to 19 out of 19 for Ca15

0.016s

Type

Details

Score

Gene

608422 | CA15

Type:	gene
Organism:	dog, domestic

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Gene

440795 | CA15P2

Type:	gene
Organism:	human

•

Gene

100996435 | CA15P1

Type:	gene
Organism:	human

•

Gene

100996556 | CA15P3

Type:	gene
Organism:	human

•

Publication

18336313 | -

First Author:	Hilvo M
Year:	2008
Journal:	Curr Pharm Des
Title:	Recent advances in research on the most novel carbonic anhydrases, CA XIII and XV.
Volume:	14
Issue:	7
Pages:	672-8

•

Protein Domain

IPR018426 | Carbonic_anhydrase_CA15

Type:

Family

Description:

Carbonic anhydrases (CA: ) are zinc metalloenzymes which catalyse the reversible hydration of carbon dioxide to bicarbonate [, ]. CAs have essential roles in facilitating the transport of carbon dioxide and protons in the intracellular space, across biological membranes and in the layers of the extracellular space; they are also involved in many other processes, from respiration and photosynthesis in eukaryotes to cyanate degradation in prokaryotes. There are five known evolutionarily distinct CA families (alpha, beta, gamma, delta and epsilon) that have no significant sequence identity and have structurally distinct overall folds. Some CAs are membrane-bound, while others act in the cytosol; there are several related proteins that lack enzymatic activity. The active site of alpha-CAs is well described, consisting of a zinc ion coordinated through 3 histidine residues and a water molecule/hydroxide ion that acts as a potent nucleophile. The enzyme employs a two-step mechanism: in the first step, there is a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide; in the second step, the active site is regenerated by the ionisation of the zinc-bound water molecule and the removal of a proton from the active site []. Beta- and gamma-CAs also employ a zinc hydroxide mechanism, although at least some beta-class enzymes do not have water directly coordinated to the metal ion. The alpha-CAs are found predominantly in animals but also in bacteria and green algae. There are at least 15 isoforms found in mammals, which can be subdivided into cytosolic CAs (CA-I, CA-II, CA-III, CA-VII and CA XIII), mitochondrial CAs (CA-VA and CA-VB), secreted CAs (CA-VI), membrane-associated (CA-IV, CA-IX, CA-XII and CA-XIV) and those without CA activity, the CA-related proteins (CA-RP VIII, X and XI).The beta-CAs are highly abundant in plants, diatoms, eubacteria and archaea [, ]. The beta-CAs are far more diverse in sequence than other classes, and can be divided into different clades based on sequence identity, with the plant enzymes forming two clades representing dicotyledonous and monocotyledonous plants. Characterisation of these enzymes reveals sharp differences between the beta class, which forms dimers, tetramers, hexamers and octomers, and the alpha and gamma classes, which form strictly monomers and trimers. The gamma-CAs may be the most ancient form of carbonic anhydrases, having evolved long before the alpha class, to which it is more closely related than to the beta-class [, ]. The reaction mechanism of the gamma-class is similar to that of the alpha-class, even though the overall folds are dissimilar and the active site residues differ. The delta-CAs are found in marine algae and dinoflagellates []. The epsilon-CAs are found in prokaryotes such as Thiobacillus neapolitanus (Halothiobacillus neapolitanus) in which it is a component of the carboxysome shell, where it could supply the active sites of RuBisCO in the carboxysome with the high concentrations of carbon dioxide necessary for optimal RuBisCO activity and efficient carbon fixation [].This entry represents carbonic anhydrase 15 enzymes. CA15 is an exceptional enzyme, as it seems to be active in numerous species, such as rodents, birds and fish, but is absent from humans and chimpanzees [, ].

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Publication

17504134 | -

First Author:	Hilvo M
Year:	2007
Journal:	Curr Top Med Chem
Title:	Characterization and inhibition of the recently discovered carbonic anhydrase isoforms CA XIII, XIV and XV.
Volume:	7
Issue:	9
Pages:	893-9

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Protein

Q8BPV2

Organism:	Mus musculus/domesticus
Length:	197
Fragment?:	false

•

Protein

Q99N23

Organism:	Mus musculus/domesticus
Length:	324
Fragment?:	false

•

Protein

Q3V275

Organism:	Mus musculus/domesticus
Length:	351
Fragment?:	false

•

Publication

9336012 | -

First Author:	Lindskog S
Year:	1997
Journal:	Pharmacol Ther
Title:	Structure and mechanism of carbonic anhydrase.
Volume:	74
Issue:	1
Pages:	1-20

•

Publication

18336305 | -

First Author:	Supuran CT
Year:	2008
Journal:	Curr Pharm Des
Title:	Carbonic anhydrases--an overview.
Volume:	14
Issue:	7
Pages:	603-14

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Publication

10978542 | -

First Author:	Smith KS
Year:	2000
Journal:	FEMS Microbiol Rev
Title:	Prokaryotic carbonic anhydrases.
Volume:	24
Issue:	4
Pages:	335-66

•

Publication

16407248 | -

First Author:	Sawaya MR
Year:	2006
Journal:	J Biol Chem
Title:	The structure of beta-carbonic anhydrase from the carboxysomal shell reveals a distinct subclass with one active site for the price of two.
Volume:	281
Issue:	11
Pages:	7546-55

•

Publication

12107142 | -

First Author:	Smith KS
Year:	2002
Journal:	J Bacteriol
Title:	Roles of the conserved aspartate and arginine in the catalytic mechanism of an archaeal beta-class carbonic anhydrase.
Volume:	184
Issue:	15
Pages:	4240-5

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Publication

18289884 | -

First Author:	Fu X
Year:	2008
Journal:	Mol Phylogenet Evol
Title:	Evolution of structure in gamma-class carbonic anhydrase and structurally related proteins.
Volume:	47
Issue:	1
Pages:	211-20

•

Publication

18336318 | -

First Author:	Zimmerman SA
Year:	2008
Journal:	Curr Pharm Des
Title:	The beta and gamma classes of carbonic anhydrase.
Volume:	14
Issue:	7
Pages:	716-21

•

Publication

18467453 | -

First Author:	Lapointe M
Year:	2008
Journal:	Plant Physiol
Title:	An external delta-carbonic anhydrase in a free-living marine dinoflagellate may circumvent diffusion-limited carbon acquisition.
Volume:	147
Issue:	3
Pages:	1427-36

•

Publication

14729686 | -

First Author:	So AK
Year:	2004
Journal:	J Bacteriol
Title:	A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a component of the carboxysome shell.
Volume:	186
Issue:	3
Pages:	623-30

•

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