Linked Life Data

17938906

Source:http://linkedlifedata.com/resource/pubmed/id/17938906

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2007-11-20
pubmed:abstractText
An NAD(+)-dependent L-arabinitol 4-dehydrogenase (LAD, EC 1.1.1.12) from Neurospora crassa was cloned and expressed in Escherichia coli and purified to homogeneity. The enzyme was a homotetramer and contained two Zn(2+) ions per subunit, displaying similar characteristics to medium-chain sorbitol dehydrogenases (SDHs). High enzymatic activity was observed for substrates L-arabinitol, adonitol, and xylitol and no activity for D-mannitol, D-arabinitol, or D-sorbitol. The enzyme showed strong preference for NAD(+) but also displayed a very low yet detectable activity with NADP(+). Mutational analysis of residue F59, the single different substrate-binding residue between LADs and D-SDHs, failed to confer the enzyme the ability to accept D-sorbitol as a substrate, suggesting that the amino acids flanking the active site cleft may be responsible for the different activity and affinity patterns between LADs and SDHs. This enzyme should be useful for in vivo and in vitro production of xylitol and ethanol from L-arabinose.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0175-7598
pubmed:author
pubmed:issnType
Print
pubmed:volume
77
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
845-52
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Cloning, characterization, and mutational analysis of a highly active and stable L-arabinitol 4-dehydrogenase from Neurospora crassa.
pubmed:affiliation
Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't