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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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 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: Published in print
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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: -