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Expression, crystallization and preliminary X-ray analysis of isomaltulose synthase (PalI) from Klebsiella sp. LX3
- Source :
- Acta crystallographica. Section D, Biological crystallography. 59(Pt 1)
- Publication Year :
- 2002
-
Abstract
- Isomaltulose synthase (PalI) catalyzes the hydrolysis of the alpha-1,2 bond between the glucose and fructose moieties of sucrose and the formation of alpha-1,6 and alpha-1,1 bonds between the two components to produce isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofranose) and trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofranose), respectively. The PalI protein has been overexpressed, purified and crystallized at 295 K using the hanging-drop vapour-diffusion method. The crystals diffract to 2.2 A resolution using synchrotron radiation and belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 59.239, b = 94.153, c = 111.294 A.
- Subjects :
- Sucrose
Isomaltulose synthase
Genetic Vectors
Molecular Sequence Data
Crystallography, X-Ray
law.invention
Hydrolysis
chemistry.chemical_compound
Isomaltulose
Structural Biology
law
Klebsiella
Escherichia coli
Amino Acid Sequence
Crystallization
Intramolecular Transferases
biology
Chemistry
Fructose
General Medicine
Klebsiella sp. LX3
Recombinant Proteins
Crystallography
biology.protein
Orthorhombic crystal system
Subjects
Details
- ISSN :
- 09074449
- Volume :
- 59
- Issue :
- Pt 1
- Database :
- OpenAIRE
- Journal :
- Acta crystallographica. Section D, Biological crystallography
- Accession number :
- edsair.doi.dedup.....5208e8b2025c910a0b73f40f1ad2e803