Title page for ETD etd-06062008-171625
|Type of Document
||Alber, Birgit E.
||Carbonic anhydrase from Methanosarcina thermophila :proposal of a new class of carbonic anhydrases and putative roles for the enzyme in anaerobic acetate catabolism
||Biochemistry and Anaerobic Microbiology
|James G, Ferry
|Dean, Dennis R.
|Gregory, Eugene M.
|Johnson, John L.
|Niehaus, Walter G. Jr.
|Date of Defense
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 Synechococcus sp.
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