Invertase
From Proteopedia
(Difference between revisions)
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- | <StructureSection load='1w2t' size=' | + | <StructureSection load='1w2t' size='450' side='right' caption='Invertase complex with raffinose (PDB code [[1w2t]]).' scene='67/676994/Cv/1'> |
== Function == | == Function == | ||
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INV is used in the food industry to produce fructose which is sweeter and does not crystallize easily. | INV is used in the food industry to produce fructose which is sweeter and does not crystallize easily. | ||
== Structural highlights == | == Structural highlights == | ||
- | The active site pocket of INV contains the catalytic residues Asp and Glu<ref>PMID:16411890</ref>. | + | The <scene name='67/676994/Cv/6'>active site pocket of INV contains the catalytic residues Asp and Glu</scene><ref>PMID:16411890</ref>. |
</StructureSection> | </StructureSection> | ||
Revision as of 12:10, 6 April 2016
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3D Structures of invertase
Updated on 06-April-2016
References
- ↑ Neumann NP, Lampen JO. Purification and properties of yeast invertase. Biochemistry. 1967 Feb;6(2):468-75. PMID:4963242
- ↑ Proels RK, Huckelhoven R. Cell-wall invertases, key enzymes in the modulation of plant metabolism during defence responses. Mol Plant Pathol. 2014 Oct;15(8):858-64. doi: 10.1111/mpp.12139. Epub 2014 May, 13. PMID:24646208 doi:http://dx.doi.org/10.1111/mpp.12139
- ↑ Alberto F, Jordi E, Henrissat B, Czjzek M. Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose. Biochem J. 2006 May 1;395(3):457-62. PMID:16411890 doi:http://dx.doi.org/BJ20051936