Abstract：
:Aldolases are a specific group of lyases that catalyze the reversible stereoselective addition of a donor compound (nucleophile) onto an acceptor compound (electrophile). Whereas most aldolases are specific for their donor compound in the aldolization reaction, they often tolerate a wide range of aldehydes as acceptor compounds. C-C bonding by aldolases creates stereocenters in the resulting aldol products. This makes aldolases interesting tools for asymmetric syntheses of rare sugars or sugar-derived compounds as iminocyclitols, statins, epothilones, and sialic acids. Besides the well-known fructose 1,6-bisphosphate aldolase, other aldolases of microbial origin have attracted the interest of synthetic bio-organic chemists in recent years. These are either other dihydroxyacetone phosphate aldolases or aldolases depending on pyruvate/phosphoenolpyruvate, glycine, or acetaldehyde as donor substrate. Recently, an aldolase that accepts dihydroxyacetone or hydroxyacetone as a donor was described. A further enlargement of the arsenal of available chemoenzymatic tools can be achieved through screening for novel aldolase activities and directed evolution of existing aldolases to alter their substrate- or stereospecifities. We give an update of work on aldolases, with an emphasis on microbial aldolases.
journal_name
Appl Microbiol Biotechnoljournal_title
Applied microbiology and biotechnologyauthors
Samland AK,Sprenger GAdoi
10.1007/s00253-006-0422-6subject
Has Abstractpub_date
2006-07-01 00:00:00pages
253-64issue
3eissn
0175-7598issn
1432-0614journal_volume
71pub_type
杂志文章,评审abstract：:The goal of sustainable production of biochemicals and biofuels has driven the engineering of microbial cell as factories that convert low-value substrates to high-value products. Xylose is the second most abundant sugar substrate in lignocellulosic hydrolysates. We analyzed the mechanisms of xylose metabolism using g...
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