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Home > Art, Film & Photography > EC 5.3.1 EC 5.3.1: Triosephosphate Isomerase, Glucose-6-Phosphate Isomerase, Altriosephosphate Isomerase, Glucose-6-Phosphate Isomerase, Aldose-Ketose Isomerases Dose-
EC 5.3.1 EC 5.3.1: Triosephosphate Isomerase, Glucose-6-Phosphate Isomerase, Altriosephosphate Isomerase, Glucose-6-Phosphate Isomerase, Aldose-Ketose Isomerases Dose-

EC 5.3.1 EC 5.3.1: Triosephosphate Isomerase, Glucose-6-Phosphate Isomerase, Altriosephosphate Isomerase, Glucose-6-Phosphate Isomerase, Aldose-Ketose Isomerases Dose-


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About the Book

Chapters: Triosephosphate Isomerase, Glucose-6-Phosphate Isomerase, Aldose-Ketose Isomerases. Source: Wikipedia. Pages: 20. Not illustrated. Free updates online. Purchase includes a free trial membership in the publisher's book club where you can select from more than a million books without charge. Excerpt: Triose-phosphate isomerase (TPI or TIM), is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. Side view of triose P isomerase monomer, active site at top center Compound C00111 at KEGG Pathway Database.Enzyme 5.3.1.1 at KEGG Pathway Database.Compound C00118 at KEGG Pathway Database. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. In humans, deficiencies in TPI are associated with a progressive, severe neurological disorder called triose phosphate isomerase deficiency. Triose phosphate isomerase deficiency is characterized by chronic hemolytic anemia. While there are various mutations that cause this disease, most include the mutation of glutamic acid at position 104 to aspartic acid. Triose phosphate isomerase is a highly efficient enzyme, performing the reaction billions of times faster than it would occur naturally in solution. The reaction is so efficient that it is said to be catalytically perfect: it is limited only by the rate the substrate can diffuse into and out of the enzyme's active site. The mechanism involves the intermediate formation of an "enediol." The changes in free energy for each step, including the transition states, have been calculated, and are displayed in the figure. The structure of TPI facilitates the co...More: http: //booksllc.net/?id=238542


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Product Details
  • ISBN-13: 9781157093480
  • Publisher: Books LLC
  • Publisher Imprint: Books LLC
  • Height: 152 mm
  • Sub Title: Triosephosphate Isomerase, Glucose-6-Phosphate Isomerase, Altriosephosphate Isomerase, Glucose-6-Phosphate Isomerase, Aldose-Ketose Isomerases Dose-
  • Width: 229 mm
  • ISBN-10: 1157093485
  • Publisher Date: 15 Sep 2010
  • Binding: Paperback
  • Spine Width: 1 mm
  • Weight: 45 gr


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EC 5.3.1 EC 5.3.1: Triosephosphate Isomerase, Glucose-6-Phosphate Isomerase, Altriosephosphate Isomerase, Glucose-6-Phosphate Isomerase, Aldose-Ketose Isomerases Dose-
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