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

BRENDA support

Refine search

Search Substrates and Products (Substrate)

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

Search term:

Results 1 - 10 of 14 > >>
EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118more no activity with crotonoyl-CoA. The enzyme preferentially reduces long-chain 2-trans-enoyl-ACP substrates (12-24 carbons). The two substrates bind to InhA via a sequential kinetic mechanism, with the preferred ordered addition of NADH and the enoyl substrate. The chemical mechanism involves stereospecific hydride transfer of the 4S hydrogen of NADH to the C3 position of the 2-trans-enoyl substrate, followed by protonation at C2 of an enzymestabilized enolate intermediate Mycobacterium tuberculosis ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118more no activity with crotonoyl-CoA. The enzyme preferentially reduces long-chain 2-trans-enoyl-ACP substrates (12-24 carbons). The two substrates bind to InhA via a sequential kinetic mechanism, with the preferred ordered addition of NADH and the enoyl substrate. The chemical mechanism involves stereospecific hydride transfer of the 4S hydrogen of NADH to the C3 position of the 2-trans-enoyl substrate, followed by protonation at C2 of an enzymestabilized enolate intermediate Mycobacterium tuberculosis ATCC 25618 ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118trans-2-decenoyl-CoA + NADH + H+ - Mycobacterium tuberculosis decanoyl-CoA + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118trans-2-decenoyl-CoA + NADH + H+ - Mycobacterium tuberculosis ATCC 25618 decanoyl-CoA + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118trans-2-dodecenoyl-CoA + NADH + H+ - Mycobacterium tuberculosis dodecanoyl-CoA + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118trans-2-dodecenoyl-CoA + NADH + H+ pre-steady state kinetics and equilibrium data of 2-trans-dodecenoyl-CoA substrate binding to InhA. The results indicate both positive homotropic cooperativity upon substrate binding to InhA, and a bimolecular association process followed by a slow isomerization of the enzyme-substrate binary complex Mycobacterium tuberculosis dodecanoyl-CoA + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118trans-2-dodecenoyl-CoA + NADH + H+ - Mycobacterium tuberculosis H37Rv dodecanoyl-CoA + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118trans-2-dodecenoyl-CoA + NADH + H+ - Mycobacterium tuberculosis ATCC 25618 dodecanoyl-CoA + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118trans-2-hexadecenoyl-CoA + NADH + H+ - Mycobacterium tuberculosis hexadecanoyl-CoA + NAD+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118trans-2-hexadecenoyl-CoA + NADH + H+ - Mycobacterium tuberculosis ATCC 25618 hexadecanoyl-CoA + NAD+ - ?
Results 1 - 10 of 14 > >>