A Plant-Type (β-Class) Carbonic Anhydrase in the Thermophilic Methanoarchaeon<i>Methanobacterium thermoautotrophicum</i>

Smith, K. Shafer; Ferry, James G.

doi:10.1128/jb.181.20.6247-6253.1999

Cited by 156 publications

(91 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The ORF-encoded protein, Cab (carbonic anhydrase beta), was expressed in E. coli, puri¢ed to electrophoretic homogeneity and found to have carbonic anhydrase activity [55]. Native gel ¢ltration chromatography estimates the molecular mass of Cab to be approximately 90 kDa [55]. The calculated subunit molecular mass is 18.9 kDa suggesting that native Cab is a tetramer in agreement with the E. coli CynT.…”

Section: Thermoautotrophicum Vhmentioning

confidence: 90%

“…Although only two archaeal carbonic anhydrases have been documented [16,55], the enzyme appears to be widespread in the two kingdoms of the Archaea domain [14]. Interestingly, a gene encoding a putative K class carbonic anhydrase has not yet been identi¢ed in the domain, consistent with the relatively recent invention of this class.…”

Section: Properties Of Isolated Carbonic Anhydrases From the Archaea mentioning

confidence: 97%

“…Subsequently, the deduced amino acid sequence of a pu-ri¢ed carbonic anhydrase from Neisseria gonorrhoeae indicated that this enzyme belongs to the K class [53]. More recently, a putative L class carbonic anhydrase gene was identi¢ed [54] from the methanoarchaeon Methanobacterium thermoautotrophicum and the enzyme was characterized and shown to have carbonic anhydrase activity [55]. Thus, the L class has now been identi¢ed in all three domains of life.…”

Section: Three Evolutionarily Distinct Classes Of Carbonic Anhydrasementioning

confidence: 99%

“…The recent discovery of the novel Q class in the Archaea domain [15] and the ¢nding that an enzyme from the L class was present in thermophilic chemolithotrophic methanoarchaea [55] led to the hypothesis that these enzymes are more central to prokaryotic metabolism than previously recognized. This was tested by performing a survey of metabolically diverse species from both the Archaea and Bacteria domains for the presence of carbonic anhydrase utilizing both activity assays and Western blotting [14].…”

Section: Carbonic Anhydrase Is Widespread In Prokaryotesmentioning

confidence: 99%

“…Recently, genome sequencing of the thermophilic, obligately chemolithoautotrophic methanoarchaeon M. thermoautotrophicum vH revealed an open reading frame with a deduced sequence 34% identical to CynT, the L class carbonic anhydrase of E. coli [54,69]. The ORF-encoded protein, Cab (carbonic anhydrase beta), was expressed in E. coli, puri¢ed to electrophoretic homogeneity and found to have carbonic anhydrase activity [55]. Native gel ¢ltration chromatography estimates the molecular mass of Cab to be approximately 90 kDa [55].…”

Section: Thermoautotrophicum Vhmentioning

confidence: 99%

See 4 more Smart Citations

Prokaryotic carbonic anhydrases

Smith¹

2000

FEMS Microbiology Reviews

102

177

View full text Add to dashboard Cite

Carbonic anhydrases catalyze the reversible hydration of CO(2) [CO(2)+H(2)Oright harpoon over left harpoon HCO(3)(-)+H(+)]. Since the discovery of this zinc (Zn) metalloenzyme in erythrocytes over 65 years ago, carbonic anhydrase has not only been found in virtually all mammalian tissues but is also abundant in plants and green unicellular algae. The enzyme is important to many eukaryotic physiological processes such as respiration, CO(2) transport and photosynthesis. Although ubiquitous in highly evolved organisms from the Eukarya domain, the enzyme has received scant attention in prokaryotes from the Bacteria and Archaea domains and has been purified from only five species since it was first identified in Neisseria sicca in 1963. Recent work has shown that carbonic anhydrase is widespread in metabolically diverse species from both the Archaea and Bacteria domains indicating that the enzyme has a more extensive and fundamental role in prokaryotic biology than previously recognized. A remarkable feature of carbonic anhydrase is the existence of three distinct classes (designated alpha, beta and gamma) that have no significant sequence identity and were invented independently. Thus, the carbonic anhydrase classes are excellent examples of convergent evolution of catalytic function. Genes encoding enzymes from all three classes have been identified in the prokaryotes with the beta and gamma classes predominating. All of the mammalian isozymes (including the 10 human isozymes) belong to the alpha class; however, only nine alpha class carbonic anhydrase genes have thus far been found in the Bacteria domain and none in the Archaea domain. The beta class is comprised of enzymes from the chloroplasts of both monocotyledonous and dicotyledonous plants as well as enzymes from phylogenetically diverse species from the Archaea and Bacteria domains. The only gamma class carbonic anhydrase that has thus far been isolated and characterized is from the methanoarchaeon Methanosarcina thermophila. Interestingly, many prokaryotes contain carbonic anhydrase genes from more than one class; some even contain genes from all three known classes. In addition, some prokaryotes contain multiple genes encoding carbonic anhydrases from the same class. The presence of multiple carbonic anhydrase genes within a species underscores the importance of this enzyme in prokaryotic physiology; however, the role(s) of this enzyme is still largely unknown. Even though most of the information known about the function(s) of carbonic anhydrase primarily relates to its role in cyanobacterial CO(2) fixation, the prokaryotic enzyme has also been shown to function in cyanate degradation and the survival of intracellular pathogens within their host. Investigations into prokaryotic carbonic anhydrase have already led to the identification of a new class (gamma) and future research will undoubtedly reveal novel functions for carbonic anhydrase in prokaryotes.

show abstract

Section: Thermoautotrophicum Vhmentioning

confidence: 90%

Section: Properties Of Isolated Carbonic Anhydrases From the Archaea mentioning

confidence: 97%

Section: Three Evolutionarily Distinct Classes Of Carbonic Anhydrasementioning

confidence: 99%

Section: Carbonic Anhydrase Is Widespread In Prokaryotesmentioning

confidence: 99%

Section: Thermoautotrophicum Vhmentioning

confidence: 99%

See 3 more Smart Citations

Prokaryotic carbonic anhydrases

Smith¹

2000

FEMS Microbiology Reviews

102

177

View full text Add to dashboard Cite

show abstract

Carbonic Anhydrases (β‐Class)

Yamashita

Mitsuhashi

Tsukihara

2004

Handbook of Metalloproteins

View full text Add to dashboard Cite

Carbonic anhydrase (CA) catalyzes the reversible hydration of CO 2 to HCO 3 − in aqueous solution. CAs are divided into three distinct classes (α‐CAs, β‐CAs, and γ‐CAs) that have little sequence homology to one another. β‐CA plays an essential role in photosynthesis, by concentrating CO 2 in the proximity of ribulose bisphosphate carboxylase/oxygenase for CO 2 fixation. Little is known about the physiological roles performed by β‐CA in nonphotosynthetic organisms. Two homologous motifs are repeated in the Porphyridium purpureum β‐CA polypeptide (55 kDa). Each motif is composed of two components: an α/β domain and an N‐terminal arm. The two motifs in a monomer are related by a pseudo twofold axis. The two monomers form a dimer with pseudo 222 symmetry. Escherichia coli β‐CA and Pisum sativum β‐CA are composed of a tetramer and an octamer respectively. The dimer of P. purpureum β‐CA resembles a tetramer of E. coli β‐CA. A dimer of P. sativum β‐CA, which resembles the monomer of P. purpureum β‐CA, is the basic building block of the octamer. Both β‐CAs from Methanobacterium thermoautotrophicum and E. coli have one zinc atom per monomer, while β‐CA from P. purpureum contains two zinc atoms per monomer. The catalytic zinc atom at each catalytic site is coordinated by four ligands in a tetrahedral manner. A possible catalytic mechanism of β‐CA based on the structure of P. purpureum CA is proposed.

show abstract

Drug Design of Zinc‐Enzyme Inhibitors

Supuran¹,

Winum²

2009

View full text Add to dashboard Cite

Limit of Liability/Disclaimer of Warranty: While the publisher and author have used their best efforts in preparing this book, they make no representations or warranties with respect to the accuracy or completeness of the contents of this book and specifically disclaim any implied warranties of merchantability or fitness for a particular purpose. No warranty may be created or extended by sales representatives or written sales materials. The advice and strategies contained herein may not be suitable for your situation. You should consult with a professional where appropriate. Neither the publisher nor author shall be liable for any loss of profit or any other commercial damages, including but not limited to special, incidental, consequential, or other damages.For general information on our other products and services or for technical support, please contact our Customer Care Department within the United States at (800) 762-2974, outside the United States at (317) 572-3993 or fax (317) 572-4002.Wiley also publishes its books in a variety of electronic formats. Some content that appears in print may not be available in electronic formats. For more information about Wiley products, visit our web site at www.wiley.com.

show abstract

A Plant-Type (β-Class) Carbonic Anhydrase in the Thermophilic MethanoarchaeonMethanobacterium thermoautotrophicum

Cited by 156 publications

References 60 publications

Prokaryotic carbonic anhydrases

Prokaryotic carbonic anhydrases

Carbonic Anhydrases (β‐Class)

Drug Design of Zinc‐Enzyme Inhibitors

Contact Info

Product

Resources

About