碩士 / 國立清華大學 / 生物技術研究所 / 93 / Sedoheptulose-1,7-bisphosphatase (SBPase) is an enzyme unique to Calvin cycle and is involved in photosynthetic carbon fixation. Gene encoding the chloroplast SBPase from Chlorella pyrenoidosa 211-8b was cloned. The coding region of this gene contains 7 exons and 6 introns. The full length cDNA is 1572 bp, with an open reading frame of 1197 bp, which can be translated into a protein with 389 amino acid residues. Comparison of the deduced amino acid sequence reveals 72.1% identity with that of Chlamydomonas reinhardtii, an eukaryotic unicellular green algae. The putative cleavage site was determined at residue 65, resulting in 36 kDa of mature protein.
The three dimensional structure of chlorella SBPase was predicted by homology modeling. The modeled structure indicates that this protein comprises of a regulatory domain and a carbon substrate domain, joined by a single polypeptide hinge. Thioredoxin regulation of this enzyme involved cysteine residues. The potentially formed disulfide bridges are indicated.
| Identifer | oai:union.ndltd.org:TW/093NTHU5108001 |
| Date | January 2005 |
| Creators | SURYANI, 林佳佳 |
| Contributors | Bandar, Hsu, 徐邦達 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 63 |
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