Source:http://linkedlifedata.com/resource/pubmed/id/11922611
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
2002-3-29
|
| pubmed:databankReference | |
| pubmed:abstractText |
We have cloned 3 novel murine cDNAs encoding proteins containing an alpha/beta hydrolase fold; a catalytic domain found in a very wide range of enzymes. These proteins belong to the prosite UPF0017 uncharacterized protein family and we have named them lung alpha/beta hydrolase 1, 2, and 3 (LABH) since they were cloned from lung cDNA. All have 9 coding exons, encoding 412, 425, and 411 residue proteins respectively (46-48 kDa); LABH1 being closely related to LABH3 having 45% identity. All 3 proteins have a single predicted amino-terminus transmembrane domain. An alignment of family members from different phyla enabled the identification of the LABH1 catalytic triad as Ser211, Asp337, and His366. mRNA expression levels of LABH1 and 3 were highest in liver and LABH2 highest in testis. These findings suggest that the LABH proteins consist of a novel family of membrane bound enzymes whose function has yet to be determined.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0006-291X
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
5
|
| pubmed:volume |
292
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
617-25
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:11922611-Amino Acid Sequence,
pubmed-meshheading:11922611-Animals,
pubmed-meshheading:11922611-Base Sequence,
pubmed-meshheading:11922611-Catalytic Domain,
pubmed-meshheading:11922611-DNA, Complementary,
pubmed-meshheading:11922611-Emphysema,
pubmed-meshheading:11922611-Humans,
pubmed-meshheading:11922611-Hydrolases,
pubmed-meshheading:11922611-Liver,
pubmed-meshheading:11922611-Lung,
pubmed-meshheading:11922611-Male,
pubmed-meshheading:11922611-Membrane Proteins,
pubmed-meshheading:11922611-Mice,
pubmed-meshheading:11922611-Molecular Sequence Data,
pubmed-meshheading:11922611-Phylogeny,
pubmed-meshheading:11922611-Protein Folding,
pubmed-meshheading:11922611-Protein Structure, Secondary,
pubmed-meshheading:11922611-Protein Structure, Tertiary,
pubmed-meshheading:11922611-Sequence Alignment,
pubmed-meshheading:11922611-Testis,
pubmed-meshheading:11922611-Tissue Distribution
|
| pubmed:year |
2002
|
| pubmed:articleTitle |
Cloning and tissue distribution of three murine alpha/beta hydrolase fold protein cDNAs.
|
| pubmed:affiliation |
Tissue Engineering Centre, Division of Investigative Science, Faculty of Medicine, Imperial College of Science, Technology and Medicine, Chelsea & Westminster Hospital, 369 Fulham Road, London SW10 9NH, United Kingdom. alasdair.edgar@ic.ac.uk
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|