| Autor: |
Menon, Nanda K., Robbins, Jeff, Der Vartanian, Marie, Patil, Daulat, Peck, Harry D., Menon, Angeli L., Robson, Robert L., Przybyla, Alan E. |
| Zdroj: |
FEBS Letters; September 1993, Vol. 331 Issue: 1-2 p91-95, 5p |
| Abstrakt: |
Two electrophoretic forms of the large subunit of the soluble periplasmic [NiFe] hydrogenase from Desulfovibrio gigashave been detected by Western analysis. The faster moving form co‐migrates with the large subunit from purified, active enzyme. Amino acid sequence and composition of the C‐terminal tryptic peptide of the large subunit from purified hydrogenase revealed that it is 15 amino acids shorter than that predicted by the nucleotide sequence. Processing of the nascent large subunit occurs by C‐terminal cleavage between His536and Val537, residues which are highly conserved among [NiFe] hydrogenases. Mutagenesis of the analogous residues, His582and Val583, in the E. colihydrogenase‐1 (HYD1) large subunit resulted in significant decrease in processing and HYD1 activity. |
| Databáze: |
Supplemental Index |
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