Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Reference

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search
Show additional data
do not include text mining results
include AMENDA results (Automatic Mining of Enzyme Data)
include FRENDA results (AMENDA + additional results, but less precise)

Search term:

<< < Results 11 - 20 of 30 > >>
download as CSV
download all results as CSV
EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87656127 Characterization of homoisocitrate dehydrogenase involved in lysine biosynthesis of an extremely thermophilic bacterium, Thermus thermophilus HB27, and evolutionary implication of beta-decarboxylating dehydrogenase J. Biol. Chem. 278 1864-1871 2003 Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 12427751
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87660907 Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of beta-decarboxylating dehydrogenase Biochem. Biophys. Res. Commun. 331 341-346 2005 Pyrococcus horikoshii 15845397
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87669109 Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus: involvement of hydrophobic dimer-dimer interaction in extremely high thermotolerance J. Bacteriol. 187 6779-6788 2005 Thermus thermophilus 16166541
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87660918 Identification of a novel trifunctional homoisocitrate dehydrogenase and modulation of the broad substrate specificity through site-directed mutagenesis Biochem. Biophys. Res. Commun. 336 596-602 2005 Deinococcus radiodurans 16139794
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87686950 RDH10 is essential for synthesis of embryonic retinoic acid and is required for limb, craniofacial, and organ development Genes Dev. 21 1113-1124 2007 Mus musculus 17473173
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87667934 Substrate specificity analysis and inhibitor design of homoisocitrate dehydrogenase Bioorg. Med. Chem. 15 1346-1355 2007 Saccharomyces cerevisiae 17116397
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87667934 Substrate specificity analysis and inhibitor design of homoisocitrate dehydrogenase Bioorg. Med. Chem. 15 1346-1355 2007 Deinococcus radiodurans 17116397
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87685232 Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae Biochemistry 47 4169-4180 2008 Saccharomyces cerevisiae 18321070
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87687988 Dynamic expression of the retinoic acid-synthesizing enzyme retinol dehydrogenase 10 (rdh10) in the developing mouse brain and sensory organs J. Comp. Neurol. 508 879-892 2008 Mus musculus 18399539
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87696220 Potassium is an activator of homoisocitrate dehydrogenase from Saccharomyces cerevisiae Biochemistry 47 10809-10815 2008 Saccharomyces cerevisiae 18785753
<< < Results 11 - 20 of 30 > >>
download as CSV
download all results as CSV