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Sedoheptulose-bisphosphatase : ウィキペディア英語版
Sedoheptulose-bisphosphatase

Sedoheptulose-bisphosphatase (also sedoheptulose-1,7-bisphosphatase or SBPase) () is an enzyme that catalyzes the removal of a phosphate group from sedoheptulose 1,7-bisphosphate to produce sedoheptulose 7-phosphate. SBPase is an example of a phosphatase, or, more generally, a hydrolase. This enzyme participates in the Calvin cycle.
==Structure==
SBPase is a homodimeric protein, meaning that it is made up of two identical subunits. The size of this protein varies between species, but is about 92,000 Da (two 46,000 Da subunits) in cucumber plant leaves. The key functional domain controlling SBPase function involves a disulfide bond between two cysteine residues. Additionally, SBPase requires the presence of magnesium (Mg2+) to be functionally active. SBPase is bound to the stroma-facing side of the thylakoid membrane in the chloroplast in a plant. Some studies have suggested the SBPase may be part of a large (900 kDa) multi-enzyme complex along with a number of other photosynthetic enzymes.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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