1ahv
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(New page: 200px<br /> <applet load="1ahv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ahv, resolution 3.1Å" /> '''STRUCTURE OF THE OCT...)
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Revision as of 17:22, 29 October 2007
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STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH 2-NITRO-P-CRESOL
Overview
BACKGROUND: Lignin degradation leads to the formation of a broad spectrum, of aromatic molecules that can be used by various fungal micro-organisms, as their sole source of carbon. When grown on phenolic compounds, Penicillium simplicissimum induces the strong impression of a, flavin-containing vanillyl-alcohol oxidase (VAO). The enzyme catalyses the, oxidation of a vast array of substrates, ranging from aromatic amines to, 4-alkyphenols. VAO is a member of a novel class of widely distributed, oxidoreductases, which use flavin adenine dinucleotide (FAD) as a cofactor, covalently bound to the protein. We have carried out the determination of, the structure of VAO in order to shed light on the most interesting, features of these novel oxidoreductases, such as the functional, significance of ... [(full description)]
About this Structure
1AHV is a [Single protein] structure of sequence from [Penicillium simplicissimum] with FAD and NCR as [ligands]. Active as [[1]], with EC number [1.1.3.13]. Full crystallographic information is available from [OCA].
Reference
Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity., Mattevi A, Fraaije MW, Mozzarelli A, Olivi L, Coda A, van Berkel WJ, Structure. 1997 Jul 15;5(7):907-20. PMID:9261083
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