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 - 7 of 7
EC Number Cofactor Commentary Reference
Show all pathways known for 2.5.1.61Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.61dipyrromethane - 685506, 707428, 737372, 737881, 739392
Show all pathways known for 2.5.1.61Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.61dipyrromethane cofactor assembly mechanism, R149 and R173 are important, cofactor is produced from the apo-enzyme with pre-uroporphyrinogen 661042
Show all pathways known for 2.5.1.61Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.61dipyrromethane in active site as shown by using Ehrlich's reagent 696120
Show all pathways known for 2.5.1.61Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.61dipyrromethane the active site possesses the unusual dipyrromethane cofactor which is extended during the reaction by the sequential addition of the four substrate molecules. The cofactor is linked covalently to the enzyme through a thioether bridge to the invariant Cys254, binding structure, overview. Hydrolysis of the linkage between the first substrate moiety and the cofactor releases the tetrapyrrole product preuroporphyrinogen. The dipyrromethane cofactor of enzyme PBGD is light-sensitive 737341
Show all pathways known for 2.5.1.61Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.61dipyrromethane the addition of one molecule of porphobilinogen to the dipyrromethane cofactor is carried out in four steps: protonation of the substrate, porphobilinogen, deamination of porphobilinogen, electrophilic addition of the deaminated substrate to the terminal pyrrole ring of the enzyme-bound dipyrromethane cofactor and deprotonation of the carbon atom at the alpha-position of the second ring of dipyrromethane 759911
Show all pathways known for 2.5.1.61Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.61dipyrromethane the enzyme possesses a dipyrromethane cofactor, which is covalently linked by a thioether bridge to the invariant cysteine residue, Cys241. The cofactor extends during the reaction by the sequential addition of the four substrate molecules, which are released as a linear tetrapyrrole product. Structure determination of the oxidized form of the dipyrromethane cofactor covalently attached to Cys241, overview. Analysis of oxidation states of the dipyrromethane cofactor and a proposed mechanism for oxidation of the dipyrromethane to dipyrromethene and subsequently dipyrromethanone 737348
Show all pathways known for 2.5.1.61Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.61dipyrromethane the residues of the domains 1 and 2 interact with the cofactor in a coordinated way to facilitate the catalytic activity 759637
Results 1 - 7 of 7