ENZYME entry: EC 4.2.1.114

Accepted Name
Methanogen homoaconitase.
Alternative Name(s)
Methanogen HACN.
Reaction catalysed
(R)-2-hydroxybutane-1,2,4-tricarboxylate <=> (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Cofactor(s)
Iron-sulfur.
Comment(s)
  • Catalyzes several reactions in the pathway of coenzyme-B biosynthesis in methanogenic archaea.
  • In contrast to EC 4.2.1.36, this enzyme can catalyze both the dehydration of (R)-homocitrate to form cis-homoaconitate and the subsequent hydration reaction that forms homoisocitrate.
  • In addition to cis-homoaconitate, the enzyme can also catalyze the hydration of the physiological substrates dihomocitrate and trihomocitrate as well as the non-physiological substrate tetrahomocitrate.
  • Cis-aconitate and threo-DL-isocitrate cannot act as substrates, and (S)-homocitrate and trans-homoaconitate act as inhibitors of the enzyme.
Cross-references
PROSITEPDOC00423
BRENDA4.2.1.114
EC2PDB4.2.1.114
ExplorEnz4.2.1.114
PRIAM enzyme-specific profiles4.2.1.114
KEGG Ligand Database for Enzyme Nomenclature4.2.1.114
IUBMB Enzyme Nomenclature4.2.1.114
IntEnz4.2.1.114
MEDLINEFind literature relating to 4.2.1.114
MetaCyc4.2.1.114
UniProtKB/Swiss-Prot
Q8TLF1, HACA_METAC;  Q58409, HACA_METJA;  Q8PZT3, HACA_METMA;  
O27668, HACA_METTH;  Q8TJM9, HACB1_METAC;  Q8TRF7, HACB2_METAC;  
Q58667, HACB_METJA;  Q8PZ49, HACB_METMA;  O26917, HACB_METTH;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.2.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.2.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-