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

BRENDA support

Refine search

Search Cofactor

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
Image of 2D Structure
Search for synonyms (with exact matching search term)

Search term:

Results 1 - 10 of 17 > >>
EC Number Cofactor Commentary Reference
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2FAD - 392556, 392560, 392570, 696361, 724345, 724389, 739932, 742487
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2FAD FAD may be released by 1 M KBr, apoprotein has no proline dehydrogenase activity but may be restored by external addition of FAD 392571
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2FAD 1.96 mol per mol of enzyme complex 658668
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2FAD flavin cofactor, 1.2fold stimulated by exogenous FAD 722591
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2ATP - 739932
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2FMN - 739932
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2[4Fe-4S]-center - 739932
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2coenzyme Q1 coenzyme Q1 is electron acceptor for PRODH/POX, which passes electrons directly to coenzyme Q1 (CoQ1) RODH/POX binds directly to CoQ1 without the formation of a tertiary complex. The transfer of electrons from proline to CoQ1 by PRODH/POX is dependent on downstream electron transfer from CoQ1 to Complexes III and IV 741588
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2FAD non-covalent binding 741732
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2FAD enzyme-bound, dependent on. Addition of excess FAD hardly improves the enzyme activity, confirming that the enzyme is fully saturated with FAD 742162
Results 1 - 10 of 17 > >>