2fbl
From Proteopedia
Jump to navigationJump to search
The crystal structure of the hypothetical protein NE1496
| ||||||||||||
Structural highlights
Function3PASE_NITEU Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The enzyme has a strong preference for linear PPPi compared with cyclic PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains polyphosphate are not hydrolyzed. It has only a slight thiamine triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity is negligible in the presence of magnesium, but a small activity is observed in the presence of manganese, in particular with GTP.[1] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
| ||||||||||||||||||||
This page was last modified 09:22, 14 February 2024.