5 Results for "

fatty acid hydratase

" in MedChemExpress (MCE) Product Catalog:
Products (5)

5 Results for "fatty acid hydratase" in MCE Product Catalog:

1
1 Cited Publications
Cat. No.: HY-W099630
CAS No.: 624-08-8
Synonyms: 9-Heptadecanol
Target:  

Endogenous Metabolite

Research Areas:  

Others

Heptadecan-9-ol is a long-chain secondary fatty alcohol. Heptadecan-9-ol functions as a plant metabolite .
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Cat. No.: HY-134136A
CAS No.: 324518-20-9
Octanoyl coenzyme A lithium is an enoyl-CoA hydratase binder. Octanoyl coenzyme A lithium binds to the active site of enoyl-CoA hydratase, occupies the binding pocket for the fatty acid tail of the enzyme's substrate, and induces a conformational shift in a flexible protein loop via its longer octanoyl chain, forming an open channel leading to the inter-trimer gap .
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Cat. No.: HY-116037A
CAS No.: 126761-43-1
Purity:  ≥98.0%
trans-10-Heptadecenoic acid is a trans-fatty acid. trans-10-Heptadecenoic acid synthesizes polyhydroxy-chain alkanoates under the action of 2, 4-dienyl-CoA reductase and Delta3, Delta2-enyl-CoA isomerase. In the absence of 2, 4-dienyl-CoA reductase, trans-10-Heptadecenoic acid is degraded by enyl-CoA hydratase II of the multifunctional enzyme (MFE). trans-10-Heptadecenoic acid leads to massive intracellular carbon outflow through reductase dependent and direct MFE dependent pathways .
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Cat. No.: HY-134136
CAS No.: 1264-52-4
Octanoyl coenzyme A is an enoyl-CoA hydratase binder. Octanoyl coenzyme A binds to the active site of enoyl-CoA hydratase, occupies the binding pocket for the fatty acid tail of the enzyme's substrate, and induces a conformational shift in a flexible protein loop via its longer octanoyl chain, forming an open channel leading to the inter-trimer gap .
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Cat. No.: HY-134136B
CAS No.: 799812-82-1
Synonyms: S-Octanoate-CoA triammonium; S-​Octanoate-coenzyme A triammonium
Research Areas:  

Others

Octanoyl coenzyme A triammonium is an enoyl-CoA hydratase binder. Octanoyl coenzyme A triammonium binds to the active site of enoyl-CoA hydratase, occupies the binding pocket for the fatty acid tail of the enzyme's substrate, and induces a conformational shift in a flexible protein loop via its longer octanoyl chain, forming an open channel leading to the inter-trimer gap .
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