Intracellular β-Carbonic Anhydrase of the Unicellular Green Alga <i>Coccomyxa</i>1

Hiltonen, Thomas; Björkbacka, Harry; Forsman, Cecilia; Clarke, Adrian K.; Samuelsson, Göran

doi:10.1104/pp.117.4.1341

Cited by 44 publications

(20 citation statements)

References 47 publications

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“…The isolation of a 180 kDa CA from leaf tissue that was composed of 28 kDa subunits may indicate that in the plant the native quaternary structure is a hexamer [7]. Association into a hexamer is consistent with other reported tertiary structures for b-CAs [16]. The secondary structure of Repeat B is predicted to have 82% a-helical characteristics.…”

Section: Expression Of a Single Repeat Produces Active Enzymesupporting

confidence: 67%

Characterization and expression of the maize β-carbonic anhydrase gene repeat regions

Tems

Burnell

2010

Plant Physiology and Biochemistry

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Section: Expression Of a Single Repeat Produces Active Enzymesupporting

confidence: 67%

Characterization and expression of the maize β-carbonic anhydrase gene repeat regions

Tems

Burnell

2010

Plant Physiology and Biochemistry

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“…Multiple isoforms of cytoplasmic CA have been found in Dunaliella species (Goyal et al 1992), Chlorella (Karlsson et al 1998), and Coccomyxa (Hiltonen et al 1998). They are less sensitive to inhibition by sulfonamide compared to periplasmic CA (Moroney et al 1987).…”

Section: Ca Function In Different Cellular Organellesmentioning

confidence: 97%

“…Subsequently, CA isozymes from pea (Kachru and Anderson 1974) tomato (Kositsin and Khalidova 1974), and lettuce (Walk and Metzner 1975) were isolated. CA isozymes are localized in plasmalemma , chloroplast (Husic and Markus 1994), mitochondria (Eriksson et al 1996), and cytoplasm (Hiltonen et al 1998). Cytoplasmic and chloroplastic isozymes of CA are present in leaves of C 3 plants with the cytosolic CA having a higher molecular mass than the chloroplastic form (Reed and Graham 1981).…”

Section: Ca Characteristics In Plantsmentioning

confidence: 98%

Carbonic anhydrase in relation to higher plants

Tiwari¹,

Kumar²,

Singh³

et al. 2005

Photosynt.

110

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The review incorporates recent information on carbonic anhydrase (CA, EC: 4.2.1.1) pertaining to types, homology, regulation, purification, in vitro stability, and biological functions with special reference to higher plants. CA, a ubiquitous enzyme in prokaryotes and higher organisms represented by four distinct families, is involved in diverse biological processes, including pH regulation, CO 2 transfer, ion exchange, respiration, and photosynthetic CO 2 fixation. CA from higher plants traces its origin with prokaryotes and exhibits compartmentalization among their organs, tissues, and cellular organelles commensurate with specific functions. In leaves, CA represents 1-20 % of total soluble protein and abundance next only to ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBPCO) in chloroplast, facilitating CO 2 supply to phosphoenolpyruvate carboxylase in C 4 and CAM plants and RuBPCO in C 3 plants. It confers special significance to CA as an efficient biochemical marker for carbon sequestration and environmental amelioration in the current global warming scenario linked with elevated CO 2 concentrations.

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“…Coccomyxa seems to lack a CCM [7]. The identified β-CA is located in the cytosol and interestingly the total CA activity of Coccomyxa is approximately 100 times higher than that of the CCM-containing alga Chlamydomonas reinhardtii [7], [8]. The specific function of β-CA in Coccomyxa ( Co -CA) is still unclear.…”

Section: Introductionmentioning

confidence: 99%

Structural Studies of β-Carbonic Anhydrase from the Green Alga Coccomyxa: Inhibitor Complexes with Anions and Acetazolamide

et al. 2011

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The β-class carbonic anhydrases (β-CAs) are widely distributed among lower eukaryotes, prokaryotes, archaea, and plants. Like all CAs, the β-enzymes catalyze an important physiological reaction, namely the interconversion between carbon dioxide and bicarbonate. In plants the enzyme plays an important role in carbon fixation and metabolism. To further explore the structure-function relationship of β-CA, we have determined the crystal structures of the photoautotroph unicellular green alga Coccomyxa β-CA in complex with five different inhibitors: acetazolamide, thiocyanate, azide, iodide, and phosphate ions. The tetrameric Coccomyxa β-CA structure is similar to other β-CAs but it has a 15 amino acid extension in the C-terminal end, which stabilizes the tetramer by strengthening the interface. Four of the five inhibitors bind in a manner similar to what is found in complexes with α-type CAs. Iodide ions, however, make contact to the zinc ion via a zinc-bound water molecule or hydroxide ion — a type of binding mode not previously observed in any CA. Binding of inhibitors to Coccomyxa β-CA is mediated by side-chain movements of the conserved residue Tyr-88, extending the width of the active site cavity with 1.5-1.8 Å. Structural analysis and comparisons with other α- and β-class members suggest a catalytic mechanism in which the movements of Tyr-88 are important for the CO2-HCO3 - interconversion, whereas a structurally conserved water molecule that bridges residues Tyr-88 and Gln-38, seems important for proton transfer, linking water molecules from the zinc-bound water to His-92 and buffer molecules.

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Intracellular β-Carbonic Anhydrase of the Unicellular Green Alga Coccomyxa1

Cited by 44 publications

References 47 publications

Characterization and expression of the maize β-carbonic anhydrase gene repeat regions

Characterization and expression of the maize β-carbonic anhydrase gene repeat regions

Carbonic anhydrase in relation to higher plants

Structural Studies of β-Carbonic Anhydrase from the Green Alga Coccomyxa: Inhibitor Complexes with Anions and Acetazolamide

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