KEGG   ENZYME: 4.2.1.36Help
Entry
EC 4.2.1.36                 Enzyme                                 

Name
homoaconitate hydratase;
homoaconitase;
cis-homoaconitase;
HACN;
Lys4;
LysF;
2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase (incorrect)
Class
Lyases;
Carbon-oxygen lyases;
Hydro-lyases
BRITE hierarchy
Sysname
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate hydro-lyase [(Z)-but-1-ene-1,2,4-tricarboxylate-forming]
Reaction(IUBMB)
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate = (Z)-but-1-ene-1,2,4-tricarboxylate + H2O [RN:R04371]
Reaction(KEGG)
Substrate
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate [CPD:C05662]
Product
(Z)-but-1-ene-1,2,4-tricarboxylate [CPD:C04002];
H2O [CPD:C00001]
Comment
Requires a [4Fe-4S] cluster for activity. The enzyme from the hyperthermophilic eubacterium Thermus thermophilus can catalyse the reaction shown above but cannot catalyse the previously described reaction, i.e. formation of (R)-homocitrate by hydration of cis-homoaconitate. The enzyme responsible for the conversion of cis-homoaconitate into (R)-homocitrate in T. thermophilus is unknown at present but the reaction can be catalysed in vitro using aconitate hydratase from pig (EC 4.2.1.3) [2].
History
EC 4.2.1.36 created 1972, modified 2007
Pathway
Lysine biosynthesis
Metabolic pathways
Microbial metabolism in diverse environments
Biosynthesis of antibiotics
Orthology
K01705  
homoaconitate hydratase
Genes
SCE: 
YDR234W(LYS4)
AGO: 
ERC: 
KLA: 
LTH: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0B02660(NCAS0B02660)
NDI: 
NDAI_0C05030(NDAI0C05030)
TPF: 
TPHA_0L01150(TPHA0L01150)
TBL: 
TBLA_0A01460(TBLA0A01460)
TDL: 
TDEL_0B01800(TDEL0B01800)
KAF: 
KAFR_0E02730(KAFR0E02730)
PPA: 
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CTP: 
COT: 
CDU: 
CTEN: 
YLI: 
CLU: 
NCR: 
NCU08898(lys-6)
NTE: 
NEUTE1DRAFT58933(NEUTE1DRAFT_58933)
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
FPU: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
VDA: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_1596114(AO090701000041)
ANG: 
ANI_1_1106134(An15g00350)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
PBN: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
TMS: 
DSQ: 
PCO: 
SHS: 
HIR: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MPR: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT59676(AGABI1DRAFT_59676)
ABV: 
AGABI2DRAFT184036(AGABI2DRAFT_184036)
CPUT: 
SLA: 
WSE: 
WIC: 
PFP: 
MGL: 
PGR: 
MLR: 
MBR: 
SRE: 
ACAN: 
PIF: 
PSOJ: 
NGR: 
ABA: 
IAL: 
MRO: 
 » show all
Taxonomy
Reference
1  [PMID:5954805]
  Authors
Strassman M, Ceci LN.
  Title
Enzymatic formation of cis-homoaconitic acid, an intermediate in lysine biosynthesis in yeast.
  Journal
J. Biol. Chem. 241 (1966) 5401-7.
Reference
2  [PMID:16524361]
  Authors
Jia Y, Tomita T, Yamauchi K, Nishiyama M, Palmer DR.
  Title
Kinetics and product analysis of the reaction catalysed by recombinant homoaconitase from Thermus thermophilus.
  Journal
Biochem. J. 396 (2006) 479-85.
Reference
3  [PMID:10714900]
  Authors
Zabriskie TM, Jackson MD.
  Title
Lysine biosynthesis and metabolism in fungi.
  Journal
Nat. Prod. Rep. 17 (2000) 85-97.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9030-68-6

DBGET integrated database retrieval system