4.2.1.18: methylglutaconyl-CoA hydratase

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For detailed information about methylglutaconyl-CoA hydratase, go to the full flat file.

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Synonyms

(3S)-methylglutaconyl-CoA hydratase, 3-methylglutaconyl CoA hydratase, 3-methylglutaconyl-CoA hydratase, 3-MG-CoA, 3-MGCoA-H, 3MGH, At4g16800, AU RNA binding protein/enoyl-Coenzyme A hydratase, AUH, HMG-CoA hydrolyase, hydratase, methylglutaconyl coenzyme A, LiuC, methylglutaconase, methylglutaconyl coenzyme A hydratase, MG-CoA hydratase, MGCH, Tb427.10.4000

ECTree

     4 Lyases

         4.2 Carbon-oxygen lyases

             4.2.1 Hydro-lyases

                4.2.1.18 methylglutaconyl-CoA hydratase

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Results	in table
699	AA Sequence
3	Application
1	CAS Registry Number
7	Cloned(Commentary)
1	Cofactor
2	Crystallization (Commentary)
59	Disease/ Diagnostics
4	General Information
4	Inhibitors
1	kcat/KM [mM/s]
2	Ki Value [mM]
18	KM Value [mM]
5	Localization
1	Metals/Ions
6	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
27	Organism
6	Pathway
12	PDB ID
2	pH Optimum
2	pH Range
15	Protein Variants
4	Purification (Commentary)
2	Reaction
1	Reaction Type
22	Reference
11	Source Tissue
4	Specific Activity [micromol/min/mg]
38	Substrates and Products (Substrate)
4	Subunits
32	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
16	Turnover Number [1/s]

Crystallization

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Crystallization on EC 4.2.1.18 - methylglutaconyl-CoA hydratase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

AUH is crystallized with a long RNA containing 24 repeats of the AUUU motif. AUH structure is determined as an asymmetric dimer of trimers with a kink in the alignment of the trimer axes, resulting in the formation of two clefts with significantly different sizes

Homo sapiens

Q13825

706650

structures refined to 2.05 and 1.1 A, in the apo form and bound to coenzyme A, respectively. The dehydration of 3-hydroxy-3-methylglutaryl CoA to 3-methylglutaconyl CoA involves Glu112 and Glu132 and likely employs the typical crotonase acid-base mechanism. Residues Tyr231 and Arg69 are key players in positioning the substrate to enable catalysis

Myxococcus xanthus

Q1D5Y4

747539