5.4.99.64: 2-hydroxyisobutanoyl-CoA mutase

This is an abbreviated version!
For detailed information about 2-hydroxyisobutanoyl-CoA mutase, go to the full flat file.

Word Map on EC 5.4.99.64

5.4.99.64

b12-dependent

aquincola

tertiaricarbonis

acyl-coa

s-3-hydroxybutyryl-coa

2-hydroxyisobutyric

chaperone

mutases

2-hydroxyisobutyrylation

isomerization

isovaleryl-coa

tert-butyl

thioester

synthesis

Reaction

Synonyms

2-hydroxyisobutyryl-CoA mutase, Btus_0469, Btus_0470, EC 5.3.3.20, HCM, HcmA, hcmAB, HcmB, RcmA, RcmB

ECTree

5 Isomerases

5.4 Intramolecular transferases

5.4.99 Transferring other groups

5.4.99.64 2-hydroxyisobutanoyl-CoA mutase

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Results	in table
2	AA Sequence
3	Application
3	Cloned(Commentary)
1	Cofactor
2	Crystallization (Commentary)
3	General Information
49	kcat/KM [mM/s]
49	KM Value [mM]
2	Molecular Weight [Da]
2	Natural Substrates/ Products (Substrates)
9	Organism
2	Pathway
3	pH Optimum
1	pH Range
16	Protein Variants
2	Purification (Commentary)
1	Reaction
7	Reference
27	Substrates and Products (Substrate)
3	Subunits
16	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
3	Temperature Range [°C]
49	Turnover Number [1/s]

General Information

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General Information on EC 5.4.99.64 - 2-hydroxyisobutanoyl-CoA mutase

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malfunction

Kyrpidia tusciae DSM 2912

D5WTR7; D5WTR8

mutase from strain DSM 2912 catalyzes isomerization of (R)-3-hydroxybutanoyl-CoA about 7000 times more efficiently than the mutase from Aquincola tertiaricarbonis L108. The most striking structural difference between the two mutases, likely determining stereospecificity, is a replacement of active-site residue Asp found in strain L108 at position 117 with Val in the enzyme from strain DSM 2912, resulting in a reversed polarity at this binding site

737504

metabolism

2 entries