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Literature summary for 4.2.1.18 extracted from

  • Bock, T.; Reichelt, J.; Mueller, R.; Blankenfeldt, W.
    The Structure of LiuC, a 3-hydroxy-3-methylglutaconyl CoA dehydratase involved in isovaleryl-CoA biosynthesis in Myxococcus xanthus, reveals insights into specificity and catalysis (2016), ChemBioChem, 17, 1658-1664 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Myxococcus xanthus

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants

Protein Variants Comment Organism
E112Q/E132Q/R69A protein is insoluble Myxococcus xanthus
E112Q/E132Q/R69A/Y231F protein is insoluble Myxococcus xanthus
E112Q/E132Q/Y231F protein is insoluble Myxococcus xanthus

Organism

Organism UniProt Comment Textmining
Myxococcus xanthus Q1D5Y4
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Myxococcus xanthus DK 1622 Q1D5Y4
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-

Synonyms

Synonyms Comment Organism
LiuC
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Myxococcus xanthus