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| PROSITE documentation PDOC00083 [for PROSITE entry PS00088] |
Manganese and iron superoxide dismutases signature
Description
Manganese superoxide dismutase (EC 1.15.1.1) (SODM) [1] is one of the three forms of an enzyme that catalyzes the dismutation of superoxide radicals. The four ligands of the manganese atom are conserved in all the known SODM sequences. These metal ligands are also conserved in the related iron form of superoxide dismutases [2,3]. We selected, as a signature, a short conserved region which includes two of the four ligands: an aspartate and a histidine.
Last update:December 2004 / Pattern and text revised.
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Technical section
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References
| 1 | Authors | Bannister J.V. Bannister W.H. Rotilio G. |
| Title | Aspects of the structure, function, and applications of superoxide dismutase. | |
| Source | CRC Crit. Rev. Biochem. 22:111-180(1987). | |
| PubMed ID | 3315461 |
| 2 | Authors | Parker M.W. Blake C.C.F. |
| Title | Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures. | |
| Source | FEBS Lett. 229:377-382(1988). | |
| PubMed ID | 3345848 |
| 3 | Authors | Smith M.W. Doolittle R.F. |
| Title | A comparison of evolutionary rates of the two major kinds of superoxide dismutase. | |
| Source | J. Mol. Evol. 34:175-184(1992). | |
| PubMed ID | 1556751 |
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