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Literature summary for 2.3.3.10 extracted from

  • Voegeli, B.; Engilberge, S.; Girard, E.; Riobe, F.; Maury, O.; Erb, T.J.; Shima, S.; Wagner, T.
    Archaeal acetoacetyl-CoA thiolase/HMG-CoA synthase complex channels the intermediate via a fused CoA-binding site (2018), Proc. Natl. Acad. Sci. USA, 115, 3380-3385 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.3.10

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop method, 18-20°C. The crystal structure of the native complex revealed a unique, shared CoA-binding site formed by both the acetoacetyl-CoA thiolase and 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase subunits thiolases (thiolases). A small scaffold protein connects the two enzymes Methanothermococcus thermolithotrophicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37500
-
 mass spectrometric sequencing Methanothermococcus thermolithotrophicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + H2O + acetoacetyl-CoA Methanothermococcus thermolithotrophicus the enzyme catalyzes a reaction in the mevalonate pathway (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
-
 ?
acetyl-CoA + H2O + acetoacetyl-CoA Methanothermococcus thermolithotrophicus DSM 2095 the enzyme catalyzes a reaction in the mevalonate pathway (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
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 ?

Organism

Organism UniProt Comment Textmining
Methanothermococcus thermolithotrophicus A0A384E143
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-
Methanothermococcus thermolithotrophicus DSM 2095 A0A384E143
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Methanothermococcus thermolithotrophicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + H2O + acetoacetyl-CoA the enzyme catalyzes a reaction in the mevalonate pathway Methanothermococcus thermolithotrophicus (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
-
 ?
acetyl-CoA + H2O + acetoacetyl-CoA the enzyme catalyzes a reaction in the mevalonate pathway Methanothermococcus thermolithotrophicus DSM 2095 (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
-
 ?

Synonyms

Synonyms Comment Organism
3-hydroxy-3-methylglutaryl (HMG)-CoA synthase
-
 Methanothermococcus thermolithotrophicus
HMG-CoA synthase
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 Methanothermococcus thermolithotrophicus
HMGCS
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 Methanothermococcus thermolithotrophicus

General Information

General Information Comment Organism
metabolism the enzyme catalyzes a reaction in the mevalonate pathway. Mevalonate is a building block of archaeal lipids. Three enzymes are involved in its biosynthesis: acetoacetyl-CoA thiolase (thiolase), 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase (HMGCS), and HMG-CoA reductase. The thiolase reaction is highly endergonic. In the thiolase/HMGCS complex, the endergonic thiolase reaction is directly coupled to the exergonic 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase reaction. A third protein spatially connects both enzymes. The two enzymes share the same substrate-binding site. Genomic information indicates that the presence of a thiolase/HMGCS complex is common in most of archaea and many bacteria Methanothermococcus thermolithotrophicus