Carbonic anhydrase from Methanosarcina thermophila: proposal of a new class of carbonic anhydrases and putative roles for the enzyme in anaerobic acetate catabolism

Carbonic anhydrase (CA) from acetate-grown Methanosarcina thermophila strain TM-1 was purified> 10,OOO-fold (22% recovery) to apparent homogeneity and a specific activity of 4,900 units mg⁻¹.The gene encoding this CA was isolated fronl a partial genomic library on a 12-kb fragment and sequenced. Comparison of the deduced anlino acid sequence with the N-terminaI sequence of the purified protein shows that the gene encodes an additional 34 N-terminal residues with properties characteristic of signal peptides in secretory proteins. The deduced amino acid sequence has no significant identity to any known CAs, but has, among others, 35% sequence identity to the first 197 deduced N-terminal amino acids of a proposed CO₂-concentrating-mechanism protein from <i>Synechococcus</i> sp. strain PCC7942.

Name thesis:degree_name

Ph. D.

Level thesis:degree_level

doctoral

Discipline thesis:degree_discipline

Biochemistry and Anaerobic Microbiology

Department dc:contributor.department

Biochemistry and Anaerobic Microbiology

Grantor dc:publisher

Virginia Tech

Year dc:date.issued

1995

Author dc:creator

• Alber, Birgit E.

Chair dc:contributor.committeechair

• Ferry, James G.

Committee members dc:contributor.committeemember

• Dean, Dennis R.
• Johnson, John L.
• Gregory, Eugene M.
• Niehaus, Walter G. Jr.

• carbonic anhydrase
• CA

Statement dc:rights

• In Copyright

Licence dc:rights.uri

• http://rightsstatements.org/vocab/InC/1.0/

Language dc:language.iso

en

Dc Identifier Other

etd-06062008-171625

OAI identifier oai:identifier

oai:vtechworks.lib.vt.edu:10919/38486