Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2006-8-1
pubmed:abstractText
An L-galactonate dehydratase and the corresponding gene were identified from the mould Hypocrea jecorina (Trichoderma reesei). This novel enzyme converts L-galactonate to L-threo-3-deoxy-hexulosonate (2-keto-3-deoxy-L-galactonate). The enzyme is part of the fungal pathway for D-galacturonic acid catabolism, a pathway which is only partly known. It is the second enzyme of this pathway after the D-galacturonic acid reductase. L-galactonate dehydratase activity is present in H. jecorina cells grown on D-galacturonic acid but absent when other carbon sources are used for growth. A deletion of the L-galactonate dehydratase gene in H. jecorina results in a strain with no growth on D-galacturonic acid. The active enzyme was produced in the heterologous host Saccharomyces cerevisiae and characterized. It exhibited activity with L-galactonate and D-arabonate where the hydroxyl group of the C2 is in L- and the hydroxyl group of the C3 is in D-configuration in the Fischer projection. However, it did not exhibit activity with D-galactonate, D-gluconate, L-gulonate or D-xylonate where the hydroxyl groups of the C2 and C3 are in different configuration.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1060-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
L-galactonate dehydratase is part of the fungal path for D-galacturonic acid catabolism.
pubmed:affiliation
VTT Biotechnology, Espoo, Finland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't