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Cited by 478

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Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases

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JAMES M. LEIPER, Joanne SANTA MARIA, Ann Chubb, Raymond J. MacAllister, Ian G. Charles, Guy Whitley, Patrick J. Vallance·1999·Biochemical Journal

Abstract

Methylarginines inhibit nitric oxide synthases (NOS). Cellular concentrations of methylarginines are determined in part by the activity of dimethylarginine dimethylaminohydrolase (DDAH; EC 3.5.3. 18). We have cloned human DDAH and identified and expressed a second novel DDAH isoform (DDAH I and II respectively). DDAH I predominates in tissues that express neuronal NOS. DDAH II predominates in tissues expressing endothelial NOS. These results strengthen the hypothesis that methylarginine concentration is actively regulated and identify molecular targets for the tissue and cell-specific regulation of methylarginine concentration.

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Metadata

Authors
LEIPER, J. M., MARIA, J. S., Chubb, A., MacAllister, R. J., Charles, I. G., Whitley, G., & Vallance, P. J.
Venue
Biochemical Journal
Publisher
Portland Press
Published
1999-09-24
Volume
343
Issue
1
Pages
209-209
ISSN
0264-6021 (ISSN-L)
OpenAlex
W2076680300
Cited by
478
References
0
FWCI
5.88
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases. https://app.cochat.ai/papers/10.1042/0264-6021:3430209
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LEIPER, J. M., MARIA, J. S., Chubb, A., MacAllister, R. J., Charles, I. G., Whitley, G., & Vallance, P. J. (1999). Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases. Biochemical Journal. https://doi.org/10.1042/0264-6021%3A3430209

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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