4.2.1.59: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase

This is an abbreviated version!
For detailed information about 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, go to the full flat file.

Reaction

Synonyms

3-hydroxyacyl-ACP dehydratase, AT5G60335, beta-hydroxyacyl-[ACP] dehydratase, Beta-hydroxyoctanoyl-ACP-dehydrase, Beta-Hydroxyoctanoyl-acyl carrier protein dehydrase, D-3-Hydroxyoctanoyl-acyl carrier protein dehydratase, Dehydratase, beta-hydroxyoctanoyl thioester, Dehydratase, D-3-hydroxyoctanoyl-[acyl carrier protein], EC 4.2.1.58, EC 4.2.1.60, EC 4.2.1.61, FabA, FabZ, fatty acid dehydratase, HaHAD1, HaHAD2

ECTree

     4 Lyases

         4.2 Carbon-oxygen lyases

             4.2.1 Hydro-lyases

                4.2.1.59 3-hydroxyacyl-[acyl-carrier-protein] dehydratase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
40041	AA Sequence
1	CAS Registry Number
4	Cloned(Commentary)
1	Crystallization (Commentary)
1	Expression
6	General Information
1	Inhibitors
6	kcat/KM [mM/s]
3	KM Value [mM]
1	Localization
3	Natural Substrates/ Products (Substrates)
7	Organism
31	Pathway
143	PDB ID
2	pH Optimum
1	pI Value
4	Protein Variants
3	Purification (Commentary)
1	Reaction
1	Reaction Type
7	Reference
4	Source Tissue
1	Specific Activity [micromol/min/mg]
23	Substrates and Products (Substrate)
2	Subunits
22	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
2	Temperature Stability [°C]

Engineering

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Engineering on EC 4.2.1.59 - 3-hydroxyacyl-[acyl-carrier-protein] dehydratase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to Protein Variants Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

F165A

Escherichia coli

P0A6Q3

mutant enzyme shows decreased ability to discriminate between varying acyl chain lengths

747496

F171A

Escherichia coli

P0A6Q3

mutant enzyme shows decreased ability to discriminate between varying acyl chain lengths

747496

F21G

Escherichia coli

P0A6Q3

the mutant contains an expanded substrate pocket. This mutant is a possible means to produce both short and long chain fatty acids

747496

F166V

Helianthus annuus

F2VYC9

the HaHAD1 F166V mutant protein has a Km for crotonyl-CoA of 0.823 mM and the Vmax 0.02161 mM/min*mg, indicatating that the mutant protein is more active with crotonyl-CoA than wild-type HaHAD1

749034