Identification of microbial dimethylarginine dimethylaminohydrolase enzymes

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Show simple item record Maria, JS Vallance, P Charles, IG Leiper, JM 2011-02-07T06:20:19Z 1999-01
dc.identifier.citation Molecular Microbiology, 1999, 33 (6), pp. 1278 - 1279
dc.identifier.issn 0950-382X
dc.identifier.other C1UNSUBMIT en_US
dc.description.abstract Arginine metabolism is an important source of energy and nitrogen in matly microbes. In this report, we present the sequence and activity of a novel microbial enzyme located in certain arginine-handling operons. The enzyme is homologous ·to mammalian dimethylarginine dimethylaminohydrolases (DDAH) and metabolizes asymmetric methylarginines to citrulline.
dc.publisher Blackwell Publishing Ltd
dc.relation.isbasedon 10.1046/j.1365-2958.1999.01580.x
dc.title Identification of microbial dimethylarginine dimethylaminohydrolase enzymes
dc.type Journal Article
dc.parent Molecular Microbiology
dc.journal.volume 6
dc.journal.volume 33
dc.journal.number 6 en_US
dc.publocation UK en_US
dc.identifier.startpage 1278 en_US
dc.identifier.endpage 1279 en_US SCI.Medical and Molecular Biosciences en_US
dc.conference Verified OK en_US
dc.for 0605 Microbiology
dc.personcode 109028
dc.percentage 100 en_US Microbiology en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US en_US
dc.location.activity en_US
dc.description.keywords NA
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
pubs.organisational-group /University of Technology Sydney/Strength - i3
utslib.copyright.status Closed Access 2015-04-15 12:17:09.805752+10
pubs.consider-herdc false
utslib.collection.history Closed (ID: 3)

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