1uv4

From Proteopedia

Revision as of 15:07, 5 November 2007

NATIVE BACILLUS SUBTILIS ARABINANASE ARB43A

Overview

Enzymes acting on polymeric substrates are frequently classified as exo or, endo, reflecting their preference for, or ignorance of, polymer chain, ends. Most biotechnological applications, especially in the field of, polysaccharide degradation, require either endo- or exo-acting hydrolases, or they harness the essential synergy between these two modes of action., Here, we have used genomic data in tandem with structure to modify, radically, the chain-end specificity of the Cellvibrio japonicus, exo-arabinanase CjArb43A. The structure of Bacillus subtilis, endo-arabinanase 43A (BsArb43A) in harness with chain-end recognition, kinetics of CjArb43A directed a rational design approach that led to the, conversion of the Cellvibrio enzyme from an exo to an endo mode of action., One of the exo-acting mutants, D35L/Q316A, displays similar activity to WT, CjArb43A and the removal of the steric block mediated by the side chains, of Gln-316 and Asp-53 at the -3 subsite confers its capacity to attack, internal glycoside bonds. This study provides a template for the, production of tailored industrial catalysts. The introduction of subtle, changes informed by comparative 3D structural and genomic data can lead to, fundamental changes in the mode of action of these enzymes.

About this Structure

1UV4 is a Single protein structure of sequence from Bacillus subtilis with CA and EDO as ligands. Active as Arabinan endo-1,5-alpha-L-arabinosidase, with EC number 3.2.1.99 Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Tailored catalysts for plant cell-wall degradation: redesigning the exo/endo preference of Cellvibrio japonicus arabinanase 43A., Proctor MR, Taylor EJ, Nurizzo D, Turkenburg JP, Lloyd RM, Vardakou M, Davies GJ, Gilbert HJ, Proc Natl Acad Sci U S A. 2005 Feb 22;102(8):2697-702. Epub 2005 Feb 11. PMID:15708971

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