3m6i
From Proteopedia
L-arabinitol 4-dehydrogenase
Structural highlights
FunctionLAD_NEUCR Catalyzes the NAD-dependent oxidation of L-arabinitol to L-xylulose in the fungal L-arabinose catabolic pathway. L-arabinose catabolism is important for using plant material as a carbon source. Not active on D-arabinitol, D-sorbitol and D-mannitol.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedL-arabinitol 4-dehydrogenase (LAD) catalyzes the conversion of l-arabinitol into l-xylulose with concomitant NAD(+) reduction. It is an essential enzyme in the development of recombinant organisms that convert l-arabinose into fuels and chemicals using the fungal l-arabinose catabolic pathway. Here we report the crystal structure of LAD from the filamentous fungus Neurospora crassa at 2.6 A resolution. In addition, we created a number of site-directed variants of N. crassa LAD that are capable of utilizing NADP(+) as cofactor, yielding the first example of LAD with an almost completely switched cofactor specificity. This work represents the first structural data on any LAD and provides a molecular basis for understanding the existing literature on the substrate specificity and cofactor specificity of this enzyme. The engineered LAD mutants with altered cofactor specificity should be useful for applications in industrial biotechnology. Structure and engineering of L-arabinitol 4-dehydrogenase from Neurospora crassa.,Bae B, Sullivan RP, Zhao H, Nair SK J Mol Biol. 2010 Sep 10;402(1):230-40. Epub 2010 Jul 22. PMID:20655316[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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