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  Two Arabidopsis threonine aldolases are nonredundant and compete with threonine deaminase for a common substrate pool

Joshi, V., Laubengayer, K. M., Schauer, N., Fernie, A. R., & Jander, G. (2006). Two Arabidopsis threonine aldolases are nonredundant and compete with threonine deaminase for a common substrate pool. Plant Cell, 18(12), 3564-3575. doi:10.1105/tpc.106.044958.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0014-2A4E-F Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0014-2A4F-D
Genre: Journal Article

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Joshi-2006-Two Arabidopsis thre.pdf (Any fulltext), 967KB
 
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 Creators:
Joshi, V.1, Author
Laubengayer, K. M.1, Author
Schauer, N.2, Author           
Fernie, A. R.2, Author           
Jander, G.1, Author
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1External Organizations, ou_persistent22              
2Central Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753339              

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Free keywords: Aldehyde-Lyases/genetics/*metabolism Arabidopsis/*enzymology/genetics Arabidopsis Proteins/genetics/*metabolism Cloning, Molecular Gene Expression Regulation, Enzymologic Gene Expression Regulation, Plant Genes, Essential Genes, Recessive Glucuronidase/metabolism Glycine Hydroxymethyltransferase/genetics/*metabolism Isoleucine/metabolism Mutation/genetics Phenotype Seedling/enzymology Seeds/enzymology Substrate Specificity Threonine/chemistry/metabolism Threonine Dehydratase/*metabolism Yeasts/cytology
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Language(s): eng - English
 Dates: 2006-12-192006
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1105/tpc.106.044958
ISSN: 1040-4651 (Print) 1040-4651 (Linking)
URI: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17172352 http://www.plantcell.org/content/18/12/3564.full.pdf
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Title: Plant Cell
Source Genre: Journal
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Pages: - Volume / Issue: 18 (12) Sequence Number: - Start / End Page: 3564 - 3575 Identifier: -