4.2.1.55: 3-hydroxybutyryl-CoA dehydratase

This is an abbreviated version!
For detailed information about 3-hydroxybutyryl-CoA dehydratase, go to the full flat file.

Word Map on EC 4.2.1.55

4.2.1.55

thiolase

crotonyl-coa

r-specific

beta-hydroxybutyryl-coa

carboxymethylproline

trans-2-enoyl-coas

enoyl-coenzyme

beta-diketones

Reaction

Synonyms

(R)-specific enoyl-CoA hydratase, CaCRT, CP 24, crotonase, D-3-Hydroxybutyryl coenzyme A dehydratase, D-3-Hydroxybutyryl-CoA dehydratase, Dehydratase, D-3-hydroxybutyryl coenzyme A, ECH 2, Enoyl coenzyme A hydrase (D), enoyl coenzyme A hydratase, enoyl-CoA hydratase 2, Ferp_1035, phaJ

ECTree

4 Lyases

4.2 Carbon-oxygen lyases

4.2.1 Hydro-lyases

4.2.1.55 3-hydroxybutyryl-CoA dehydratase

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Results	in table
781	AA Sequence
1	CAS Registry Number
4	Cloned(Commentary)
1	Crystallization (Commentary)
4	General Information
5	Inhibitors
1	Ki Value [mM]
4	KM Value [mM]
6	Natural Substrates/ Products (Substrates)
7	Organism
12	Pathway
6	PDB ID
2	pH Optimum
3	Protein Variants
2	Purification (Commentary)
2	Reaction
2	Reaction Type
7	Reference
2	Source Tissue
2	Specific Activity [micromol/min/mg]
16	Substrates and Products (Substrate)
4	Subunits
18	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]

Subunits

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Subunits on EC 4.2.1.55 - 3-hydroxybutyryl-CoA dehydratase

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hexamer

2 entries

homodimer

Rattus norvegicus

2-enoyl-CoA hydratase 2 is the middle part of the MFP-2, the enzyme is a homodimer, unlike the mitochondrial 2-enoyl-CoA hydratase 1 that is a hexamer

694522

additional information

Clostridium acetobutylicum

the CaCRT monomer consists of an N-terminal (NTD) and a C-terminal domains (CTD). The NTD (beta1-beta7 and alpha1-alpha9) harbors the canonical crotonase fold, where a large beta-sheet (beta1-beta4 and b6) is organized with a small beta-sheet (beta5 and beta7) forming two perpendicular beta-sheets. The CTD consists of three alpha-helices (alpha10-alpha12), and this domain mediates the oligomerization of CaCRT. Additionally, the extended alpha-helix (lphaa12) interacts with the NTD of a neighboring monomer and participates in the formation of its substrate binding site. The CTDs of six monomers participate mainly in the formation of the hexameric interface

746965