The Interaction of Sulfate with Carbonic Anhydrase

Simonsson, Ingvar; Lindskog, Sven

doi:10.1111/j.1432-1033.1982.tb06494.x

Cited by 89 publications

(41 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast, spectroscopic and kinetic studies have suggested sulfate binding to both native and cobalt-substituted carbonic anhydrase (Lindskog, 1982;Simonsson & Lindskog, 1982;Pocker & Miao, 1987;Bertini, Canti, Luchinat & Scozzafava, 1977). Simonsson & Lindskog (1982) found that the esterase inhibition of sulfate never exceeded 20%, since the dissociation constant apparently increased with increasing sulfate concentration (ionic strength). Such a low degree of binding is difficult to observe crystallographically.…”

Section: Discussionmentioning

confidence: 99%

X-ray analysis of metal-substituted human carbonic anhydrase II derivatives

Håkansson¹,

Wehnert²,

Liljas³

1994

Acta Cryst D

View full text Add to dashboard Cite

Metal-substituted crystals of human carbonic anhydrase II belonging to space group P2[1 with cell dimensions a = 42.7, b = 41.7, c = 73.0A and /3 = 104.6 ° were analyzed crystallographically. The resolution limit ranged from 1.82 to 1.92A with high completeness (86.2-90.7%). Cobalt(II)-substituted carbonic anhydrase has a tetrahedral coordination around the metal both at pH 6 and pH 7.8, similar to the native zinc enzyme. In contrast, the catalytically inactive copper(II), nickel(II) and manganese(II) derivatives showed increased coordination number around the metal ion. Whereas the copper is best described as penta-coordinated, the nickel and manganese are best described as hexa-coordinated. The results are briefly compared with spectroscopic observations and our current view on carbonic anhydrase catalysis.

show abstract

Section: Discussionmentioning

confidence: 99%

X-ray analysis of metal-substituted human carbonic anhydrase II derivatives

Håkansson¹,

Wehnert²,

Liljas³

1994

Acta Cryst D

View full text Add to dashboard Cite

show abstract

“…The I,,, values correspond to the concentrations giving 50% inhibition. (Simonsson and Lindskog, 1982) and the dissociation constant for C1-is 190 mM at pH 6.8 (Behravan et al, 1990).…”

Section: Resultsmentioning

confidence: 99%

Kinetic studies of pea carbonic anhydrase

Johansson

Forsman

1993

European Journal of Biochemistry

View full text Add to dashboard Cite

Chloroplast carbonic anhydrase from Pisurn sativurn has been isolated. The kinetic properties of the enzyme have been studied and comparisons to the well characterised human carbonic anhydrase I1 made. Pea carbonic anhydrase was found to be dependent on a reducing agent in order to retain the catalytic activity. Oxidised, inactive, enzyme could be activated by the addition of a SH-agent.However, such activation gave only 60% of the activity of an enzyme kept in a reduced state all the time. The kinetics of CO, hydration show an increase in k,,, as well as in k,,,/K,,, with pH, but the pH profile does not follow a simple titration curve. The pH dependence is more complicated and it seems as if there are several titratable groups affecting the activity. At pH 9 we obtain a turnover number of 4x10' s-' and a k,,,/K,,, value of 1.8X10HM-' s-' with reference to the subunit. We also find that the enzyme needs high concentrations of buffer to work at a maximal rate. Apparent K, values with respect to the total buffer concentration are found between 52-185 mM at neutral and high pH. At low pH the situation is complex with deviations from Michaelis-Menten kinetics.Chloroplast carbonic anhydrase from higher plants have been reported to have primary structures that are completely different from the enzyme from animals. In addition, we find the circular dichroic spectrum of pea carbonic anhydrase to be well distinguished from that of human carbonic anhydrase 11. Despite those structural differences the kinetic parameters indicate that pea carbonic anhydrase is equally efficient as human carbonic anhydrase I1 in catalysing the hydration of CO, However, the mechanism for proton transfer from the active site to the surrounding medium seems to differ between the two enzymes.Carbonic anhydrase (CA; carbonate hydro-lyase) is a zinc-containing enzyme catalysing the reversible hydration of CO,. It is ubiquitous and found in vertebrates, invertebrates, higher plants, algae and in some bacteria. According to the primary structures it seems as if CA has appeared twice during evolution and thus can be divided into two groups. The first group, which is the most studied, contains all so-far-known animal isozymes and the periplasmic CA from Chlarnydomonas reinhardtii. The second group includes chloroplast CA from higher plants together with CA found in two procaryotes. The amino acid sequences for the animal CAs are found to be highly similar with several conserved regions, including the three histidine ligands of the catalytically active zinc ion (Venta et al., 1987). A water molecule is found as the fourth ligand, giving an almost tetrahedral coordination geometry around the zinc ion. In mammals seven different isozymes are known, where most interest has been focused on human CA I and I1 (HCA I and HCA 11) and bovine CA 111. These are monomers with molecular masses around 29 kDa. Their crystal structures have been solved at 0.2-nm resolution or higher and the folding of the polypeptide chain was found to be very similar for all three K...

show abstract

“…The pH/rate profile for this esterase activity shows a ply, of 6.7 (Fig. 41, whereas the corresponding value for human isozyme I1 is 6.8 [33].…”

Section: Discussionmentioning

confidence: 99%

The Complete Sequence, Expression in Escherichia Coli, Purification and Some Properties of Carbonic Anhydrase from Neisseria Gonorrhoeae

Chirică¹,

Elleby²,

Jonsson³

et al. 1997

European Journal of Biochemistry

Self Cite

View full text Add to dashboard Cite

The complete nucleotide sequence of the carbonic anhydrase gene from Neisseria gonorrhoeae has been determined. The gene encodes a 252-residue polypeptide with a molecular mass of 28085 Da. The gene has been cloned and overexpressed in Escherichia coli, and the enzyme has been purified. A 26-residue signal peptide is cleaved off by the E. coli processing machinery. Thus, the isolated enzyme contains 226 amino acid residues with a molecular mass of 25 314 Da. Most of the enzyme seems to be produced as a soluble protein located in the periplasm of E. coli. The enzyme is homologous to carbonic anhydrases from the animal kingdom; it is an a-carbonic anhydrase. A comparison with the amino acid sequences of human carbonic anhydrases I and I1 suggests that the secondary structures are essentially intact in the bacterial enzyme but that several loops are much shorter than in the human forms. Most of the active-site residues are identical to those found in the high-activity human isozyme 11. The bacterial enzyme has a high CO, hydration activity with a k,,, of 1.1 . lo6 s-' and K,, of 20 mM at pH 9 and 25°C.The enzyme also catalyzes the hydrolysis of 4-nitrophenyl acetate. The pH/rate profile can be described as a titration curve with pK, of 6.7 and a maximal value of the catalytic second-order rate constant, k,,,,,

show abstract

The Interaction of Sulfate with Carbonic Anhydrase

Cited by 89 publications

References 34 publications

X-ray analysis of metal-substituted human carbonic anhydrase II derivatives

X-ray analysis of metal-substituted human carbonic anhydrase II derivatives

Kinetic studies of pea carbonic anhydrase

The Complete Sequence, Expression in Escherichia Coli, Purification and Some Properties of Carbonic Anhydrase from Neisseria Gonorrhoeae

Contact Info

Product

Resources

About