1qrm

Structural highlights

Function

CAH_METTT Reversible hydration of carbon dioxide. Important for growth on acetate (PubMed:8041719). As a probably extracellular enzyme, it may support a H(+)/CH(3)COO(-) symport mechanism and/or conversion of CO(2) to HCO(3)(-), removing excess CO(2) produced by growth on acetate (Probable).^{[1] [2] [3] [4]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Carbonic anhydrase 3D structures

References

1. ↑ Alber BE, Ferry JG. A carbonic anhydrase from the archaeon Methanosarcina thermophila. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):6909-13. PMID:8041719
2. ↑ Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC. A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry. 2000 Aug 8;39(31):9222-31. PMID:10924115
3. ↑ Alber BE, Ferry JG. A carbonic anhydrase from the archaeon Methanosarcina thermophila. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):6909-13. PMID:8041719
4. ↑ Kisker C, Schindelin H, Alber BE, Ferry JG, Rees DC. A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila. EMBO J. 1996 May 15;15(10):2323-30. PMID:8665839