1a80: Difference between revisions
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'''NATIVE 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE A FROM CORYNBACTERIUM SP. COMPLEXED WITH NADPH''' | '''NATIVE 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE A FROM CORYNBACTERIUM SP. COMPLEXED WITH NADPH''' | ||
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[[Category: Powers, D B.]] | [[Category: Powers, D B.]] | ||
[[Category: 2,5-diketo-d-gluconic acid]] | [[Category: 2,5-diketo-d-gluconic acid]] | ||
[[Category: | [[Category: Alpha8/beta8 barrel]] | ||
[[Category: | [[Category: Commercial vitamin c synthesis]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:57:10 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 09:57, 2 May 2008
NATIVE 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE A FROM CORYNBACTERIUM SP. COMPLEXED WITH NADPH
OverviewOverview
The three-dimensional structure of Corynebacterium 2, 5-diketo-D-gluconic acid reductase A (2,5-DKGR A; EC 1.1.1.-), in complex with cofactor NADPH, has been solved by using x-ray crystallographic data to 2.1-A resolution. This enzyme catalyzes stereospecific reduction of 2,5-diketo-D-gluconate (2,5-DKG) to 2-keto-L-gulonate. Thus the three-dimensional structure has now been solved for a prokaryotic example of the aldo-keto reductase superfamily. The details of the binding of the NADPH cofactor help to explain why 2,5-DKGR exhibits lower binding affinity for cofactor than the related human aldose reductase does. Furthermore, changes in the local loop structure near the cofactor suggest that 2,5-DKGR will not exhibit the biphasic cofactor binding characteristics observed in aldose reductase. Although the crystal structure does not include substrate, the two ordered water molecules present within the substrate-binding pocket are postulated to provide positional landmarks for the substrate 5-keto and 4-hydroxyl groups. The structural basis for several previously described active-site mutants of 2,5-DKGR A is also proposed. Recent research efforts have described a novel approach to the synthesis of L-ascorbate (vitamin C) by using a genetically engineered microorganism that is capable of synthesizing 2,5-DKG from glucose and subsequently is transformed with the gene for 2,5-DKGR. These modifications create a microorganism capable of direct production of 2-keto-L-gulonate from D-glucose, and the gulonate can subsequently be converted into vitamin C. In economic terms, vitamin C is the single most important specialty chemical manufactured in the world. Understanding the structural determinants of specificity, catalysis, and stability for 2,5-DKGR A is of substantial commercial interest.
About this StructureAbout this Structure
1A80 is a Single protein structure of sequence from Corynebacterium sp.. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-A resolution., Khurana S, Powers DB, Anderson S, Blaber M, Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6768-73. PMID:9618487 Page seeded by OCA on Fri May 2 09:57:10 2008