4.1.3.4: hydroxymethylglutaryl-CoA lyase
This is an abbreviated version!
For detailed information about hydroxymethylglutaryl-CoA lyase, go to the full flat file.
Word Map on EC 4.1.3.4
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4.1.3.4
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3-hydroxy-3-methylglutaric
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aciduria
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ketogenesis
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hypoglycemia
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acidosis
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inborn
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3-methylglutaric
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3-methylglutaconic
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ketogenic
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3-hydroxyisovaleric
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hyperammonemia
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hypoketotic
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mevalonii
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lethargy
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3-methylcrotonyl-coa
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medicine
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acetoacetyl-coa
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hl-deficient
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hmgcs2
- 4.1.3.4
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3-hydroxy-3-methylglutaric
- aciduria
-
ketogenesis
- hypoglycemia
- acidosis
-
inborn
-
3-methylglutaric
-
3-methylglutaconic
-
ketogenic
-
3-hydroxyisovaleric
-
hyperammonemia
-
hypoketotic
- mevalonii
- lethargy
- 3-methylcrotonyl-coa
- medicine
- acetoacetyl-coa
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hl-deficient
- hmgcs2
Reaction
Synonyms
3-hydroxy-3-methylglutarate-CoA lyase, 3-Hydroxy-3-methylglutaryl CoA cleaving enzyme, 3-hydroxy-3-methylglutaryl CoA lyase, 3-Hydroxy-3-methylglutaryl coenzyme A lyase, 3-Hydroxy-3-methylglutaryl-CoA lyase, 3-hydroxy-3-methylglutaryl-CoA lyase-like protein, 3-hydroxy-3-methylglutaryl-coenzyme A lyase, 3-hydroxy-methylglutaryl coenzyme A lyase, beta-hydroxy-beta-methylglutaryl-CoA lyase, HCL1, HL, HMG CoA cleavage enzyme, HMG CoA lyase, HMG-CoA lyase, HMGCL, HMGCLL1, HMGL, Hydroxymethylglutaryl coenzyme A lyase, Hydroxymethylglutaryl coenzyme A-cleaving enzyme, LiuE protein
ECTree
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Metals Ions
Metals Ions on EC 4.1.3.4 - hydroxymethylglutaryl-CoA lyase
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Bivalent cations
Cu2+
Mg2+
Mn2+
additional information
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possibly involved in coordination of the thioesther carbonyl during catalysis, also stimulates acetyl-CoA enolization
Mg2+
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required, Km for wild-type HMGCL is 0.233 mM and for HMGCL mutant C323A 0.322 mM
Mg2+
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required, Km of wild-type HMGCLL1 is 0.049 mM and for HMGCLL1 mutant G2A 0.088 mM
Mn2+
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required, Km for wild-type HMGCL is 0.00034 mM and for HMGCL mutant C323A 0.00037 mM
Mn2+
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required, Km of wild-type HMGCLL1 is 0.00018 mM and for HMGCLL1 mutant G2A 0.00024 mM
reaction mechanism involves an invariant Asp-Arg-Glu (DRE)triplet. The Asp ligates the divalent cation, the Arg probably stabilizes charge accumulation in the enolate intermediate, and the Glu maintains the precise structural alignment of the Asp and Arg
additional information
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reaction mechanism involves an invariant Asp-Arg-Glu (DRE)triplet. The Asp ligates the divalent cation, the Arg probably stabilizes charge accumulation in the enolate intermediate, and the Glu maintains the precise structural alignment of the Asp and Arg
additional information
reaction mechanism involves an invariant Asp-Arg-Glu (DRE)triplet. The Asp ligates the divalent cation, the Arg probably stabilizes charge accumulation in the enolate intermediate, and the Glu maintains the precise structural alignment of the Asp and Arg
additional information
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reaction mechanism involves an invariant Asp-Arg-Glu (DRE)triplet. The Asp ligates the divalent cation, the Arg probably stabilizes charge accumulation in the enolate intermediate, and the Glu maintains the precise structural alignment of the Asp and Arg
additional information
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identification of His233, His235, ASp42, and Asn275 as metal-binding ligands