Sedoheptulose-1,7-biphosphatase (SBPase) 是卡爾文氏循環特有的酵素，並且參與光合作用的固碳反應。小球藻的SBPase染色體基因包含7個exon和6個intron。它的cDNA全長有1572 bp，其中有1197 bp是開放讀碼區 (ORF)，可轉譯為389個胺基酸。胺基酸序列的比對顯示小球藻與Chlamydomonas reinhardtii的SBPase有72.1%的相似度。小球藻SBPase的putative cleavage site估計在第65胺基酸，而產生36 kDa的成熟蛋白質。
利用homology modeling預測小球藻SBPase酵素的三級結構顯示此蛋白質有兩個區域，調控區域和受質區域，而兩個區域以單條多胜鍵形成的轉接摳扭連接在一起。此酵素的鐵硫氧化還原蛋白(thioredoxin) 調控與半胱胺基酸有關。在小球藻SBPase蛋白質裡發現相近的半胱胺基酸有潛力形成雙硫鍵。

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.

吳欣欣 (2002) 小球藻熱逆境後葉綠素和葉綠體衰變的研究，國立清華大學生命科學研究所碩士論文

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