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Structural studies of the final enzyme in the alpha-aminoadipate pathway-saccharopine dehydrogenase from Saccharomyces cerevisiae.

Abstract：

:The 1.64 A structure of the apoenzyme form of saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae shows the enzyme to be composed of two domains with similar dinucleotide binding folds with a deep cleft at the interface. The structure reveals homology to alanine dehydrogenase, despite low primary sequence similarity. A model of the ternary complex of SDH, NAD, and saccharopine identifies residues Lys77 and Glu122 as potentially important for substrate binding and/or catalysis, consistent with a proton shuttle mechanism. Furthermore, the model suggests that a conformational change is required for catalysis and that residues Lys99 and Asp281 may be instrumental in mediating this change. Analysis of the crystal structure in the context of other homologous enzymes from pathogenic fungi and human sources sheds light into the suitability of SDH as a target for antimicrobial drug development.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Burk DL,Hwang J,Kwok E,Marrone L,Goodfellow V,Dmitrienko GI,Berghuis AM

doi

10.1016/j.jmb.2007.08.044

subject

Has Abstract

pub_date

2007-10-26 00:00:00

pages

745-54

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(07)01115-1

journal_volume

373

pub_type

杂志文章

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