enzyme:1.1.1.n12 : No such data.

KEGG   ENZYME: 4.2.1.107Help
Entry
EC 4.2.1.107                Enzyme                                 

Name
3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase;
46 kDa hydratase 2;
(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA hydro-lyase
Class
Lyases;
Carbon-oxygen lyases;
Hydro-lyases
BRITE hierarchy
Sysname
(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA hydro-lyase [(24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA-forming]
Reaction(IUBMB)
(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O [RN:R04813]
Reaction(KEGG)
Substrate
(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA
Product
(24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA;
H2O [CPD:C00001]
Comment
This enzyme forms part of the rat peroxisomal multifunctional enzyme perMFE-2, which also exhibits a dehydrogenase activity. The enzyme is involved in the beta-oxidation of the cholesterol side chain in the cholic-acid-biosynthesis pathway.
History
EC 4.2.1.107 created 2005
Pathway
Primary bile acid biosynthesis
Metabolic pathways
Orthology
K08078  
3a,7a,12a-trihydroxy-5b-cholest-24-enoyl-CoA hydratase
K12405  
3-hydroxyacyl-CoA dehydrogenase / 3a,7a,12a-trihydroxy-5b-cholest-24-enoyl-CoA hydratase
Genes
HSA: 
3295(HSD17B4)
PTR: 
462019(HSD17B4)
PPS: 
100981028(HSD17B4)
GGO: 
PON: 
100448539(HSD17B4)
MCC: 
698369(HSD17B4)
MCF: 
102123675(HSD17B4)
MMU: 
15488(Hsd17b4)
RNO: 
79244(Hsd17b4)
HGL: 
101713520(Hsd17b4)
TUP: 
102468828(HSD17B4)
CFA: 
474630(HSD17B4)
AML: 
100471749(HSD17B4)
FCA: 
101091840(HSD17B4)
PTG: 
102968873(HSD17B4)
BTA: 
493643(HSD17B4)
BOM: 
102268517(HSD17B4)
PHD: 
102329357(HSD17B4)
CHX: 
102172142(HSD17B4)
SSC: 
397574(HSD17B4)
CFR: 
102508317(HSD17B4)
ECB: 
100034046(HSD17B4)
MYB: 
102240475(HSD17B4)
MYD: 
102767159(HSD17B4)
PALE: 
102887000(HSD17B4)
MDO: 
100028098(HSD17B4)
SHR: 
100932771(HSD17B4)
OAA: 
100081754(HSD17B4)
GGA: 
395785(HSD17B4)
MGP: 
TGU: 
100218226(HSD17B4)
FAB: 
101807233(HSD17B4)
PHI: 
102109547(HSD17B4)
APLA: 
101791118(HSD17B4)
FPG: 
101917400(HSD17B4)
FCH: 
102058406(HSD17B4)
CLV: 
102095771(HSD17B4)
ASN: 
102371766(HSD17B4)
PSS: 
102451304(HSD17B4)
CMY: 
102933522(HSD17B4)
ACS: 
100558484(hsd17b4)
XLA: 
444492(hsd17b4)
XTR: 
613082(hsd17b4)
DRE: 
393105(hsd17b4)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102356548(HSD17B4)
BFO: 
CIN: 
100187421(hsd17b4)
SPU: 
581580(hsd17b4)
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
409986(GB18162)
NVI: 
TCA: 
663655(17-beta-HD4)
BMOR: 
API: 
PHU: 
ISC: 
CBR: 
CBG10899(Cbr-dhs-28) CBG13089(Cbr-maoc-1)
BMY: 
LOA: 
NVE: 
HMG: 
TAD: 
AQU: 
100640903(Hsd17b4)
MBR: 
DDI: 
DPP: 
DFA: 
DFA_02002(mfeA)
ACAN: 
TGO: 
TET: 
PIF: 
NGR: 
PRE: 
SSE: 
ACR: 
DRM: 
 » show all
Taxonomy
Reference
1  [PMID:9371691]
  Authors
Qin YM, Haapalainen AM, Conry D, Cuebas DA, Hiltunen JK, Novikov DK.
  Title
Recombinant 2-enoyl-CoA hydratase derived from rat peroxisomal multifunctional enzyme 2: role of the hydratase reaction in bile acid synthesis.
  Journal
Biochem. J. 328 ( Pt 2) (1997) 377-82.
  Organism
Rattus norvegicus
Reference
2  [PMID:8619845]
  Authors
Xu R, Cuebas DA.
  Title
The reactions catalyzed by the inducible bifunctional enzyme of rat liver peroxisomes cannot lead to the formation of bile acids.
  Journal
Biochem. Biophys. Res. Commun. 221 (1996) 271-8.
  Organism
Rattus norvegicus
Reference
3
  Authors
Kinoshita, T., Miyata, M., Ismail, S.M., Fujimoto, Y., Kakinuma, K., Kokawa, N.I. and Morisaki, M.
  Title
Synthesis and determination of stereochemistry of four diastereoisomers at the C-24 and C-25 positions of 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oic acid and cholic acid.
  Journal
Chem. Pharm. Bull. 36 (1988) 134-141.
Reference
4
  Authors
Fujimoto, Y., Kinoshita, T., Oya, I., Kakinuma, K., Ismail, S.M., Sonoda, Y., Sato, Y. and Morisaki, M.
  Title
Non-stereoselective conversion of the four diastereoisomers at the C-24 and C-25 positions of 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oic acid and cholic acid.
  Journal
Chem. Pharm. Bull. 36 (1988) 142-145.
Reference
5  [PMID:11146090]
  Authors
Kurosawa T, Sato M, Nakano H, Fujiwara M, Murai T, Yoshimura T, Hashimoto T.
  Title
Conjugation reactions catalyzed by bifunctional proteins related to beta-oxidation in bile acid biosynthesis.
  Journal
Steroids. 66 (2001) 107-14.
  Organism
Rattus norvegicus
Reference
6  [PMID:12543708]
  Authors
Russell DW.
  Title
The enzymes, regulation, and genetics of bile acid synthesis.
  Journal
Annu. Rev. Biochem. 72 (2003) 137-74.
  Organism
Homo sapiens
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
152787-68-3

KEGG   ENZYME: 4.2.1.119Help
Entry
EC 4.2.1.119                Enzyme                                 

Name
enoyl-CoA hydratase 2;
2-enoyl-CoA hydratase 2;
AtECH2;
ECH2;
MaoC;
MFE-2;
PhaJAc;
D-3-hydroxyacyl-CoA hydro-lyase;
D-specific 2-trans-enoyl-CoA hydratase
Class
Lyases;
Carbon-oxygen lyases;
Hydro-lyases
BRITE hierarchy
Sysname
(3R)-3-hydroxyacyl-CoA hydro-lyase
Reaction(IUBMB)
(3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA + H2O [RN:R09698]
Reaction(KEGG)
Substrate
(3R)-3-hydroxyacyl-CoA [CPD:C01086]
Product
(2E)-2-enoyl-CoA [CPD:C00658];
H2O [CPD:C00001]
Comment
This enzyme catalyses a hydration step in peroxisomal beta-oxidation. The human multifunctional enzyme type 2 (MFE-2) is a 79000 Da enzyme composed of three functional units: (3R)-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and sterol carrier protein 2-like units [1]. The enzymes from Aeromonas caviae [4] and Arabidopsis thaliana [5] are monofunctional enzymes. 2-Enoyl-CoA hydratase 3 from Candida tropicalis is a part from multifunctional enzyme type 2 [3].
History
EC 4.2.1.119 created 2009
Orthology
K08299  
crotonobetainyl-CoA hydratase
Genes
ECO: 
b0036(caiD)
ECJ: 
Y75_p0036(caiD)
ECD: 
EBW: 
BWG_0034(caiD)
ECOK: 
ECE: 
Z0042(caiD)
ECS: 
ECF: 
ETW: 
ECSP_0039(caiD)
ELX: 
EOJ: 
EOI: 
EOH: 
ECG: 
EOK: 
ELR: 
ECC: 
c0045(caiD)
ECP: 
ECI: 
ECV: 
ECX: 
ECW: 
ECM: 
ECY: 
ECR: 
ECQ: 
ECK: 
ECT: 
EOC: 
CE10_0037(caiD)
EUM: 
ECZ: 
ELO: 
ELN: 
ELH: 
ESE: 
ESO: 
ESM: 
ESL: 
ECL: 
EBR: 
ECB_00040(caiD)
EBD: 
EKO: 
EKF: 
EAB: 
EDH: 
EDJ: 
EIH: 
ENA: 
ELU: 
EUN: 
ELW: 
ECW_m0036(caiD)
ELL: 
WFL_00180(caiD)
ELC: 
i14_0038(caiD)
ELD: 
i02_0038(caiD)
ELP: 
EBL: 
ECD_00040(caiD)
EBE: 
B21_00039(caiD)
ELF: 
LF82_0260(caiD)
ECOA: 
ECOL: 
ECOI: 
ECOJ: 
ECOO: 
EFE: 
EFER_0044(caiD)
EBT: 
STY: 
STY0080(caiD)
STT: 
t0071(caiD)
SEX: 
SENT: 
STM: 
STM0070(caiD)
SEO: 
SEV: 
SEY: 
SEM: 
SEJ: 
SEB: 
SEF: 
SETU: 
SETC: 
SEEN: 
SENR: 
SEND: 
SPT: 
SPA0071(caiD)
SEK: 
SPQ: 
SEI: 
SPC_0075(caiD)
SEC: 
SC0064(caiD)
SEH: 
SHB: 
SENH: 
SEEH: 
SEE: 
SENN: 
SEW: 
SEA: 
SENS: 
SED: 
SEG: 
SG0073(caiD)
SEL: 
SPUL_0075(caiD)
SEGA: 
SET: 
SEN0071(caiD)
SENJ: 
SEEC: 
SEEB: 
SEEP: 
SENB: 
BN855_730(SBOV00171)
SENE: 
SES: 
SBG: 
SBG_0055(caiD)
SBZ: 
SFL: 
SF0033(caiD)
SFX: 
S0035(caiD)
SFV: 
SFV_0030(caiD)
SFE: 
SFxv_0034(caiD)
SSN: 
SSON_0042(caiD)
SSJ: 
SDY: 
SDY_0058(caiD)
SDZ: 
ESC: 
CKO: 
CRO: 
ROD_00381(caiD)
SMAF: 
PMR: 
PMI2658(caiD)
PMIB: 
EIC: 
ETR: 
ETAE_2660(caiD)
ETD: 
ETC: 
EBF: 
XAL: 
PSO: 
ACI: 
ACIAD1571(caiD)
SLO: 
SSE: 
SPL: 
SHL: 
SWP: 
GAG: 
ADI: 
B5T_02472(fadB2)
BCH: 
BCM: 
BCJ: 
BCAM2695(caiD)
BXE: 
BYI: 
VEI: 
VPD: 
MLO: 
MCI: 
MOP: 
MAM: 
PLA: 
SME: 
SMK: 
SMQ: 
SMX: 
SMI: 
SMEG: 
SMEL: 
SMD: 
RHI: 
SFH: 
SFD: 
ARA: 
RET: 
REL: 
RLE: 
RLT: 
RLG: 
RLB: 
RTR: 
BPP: 
BPI_II563(caiD)
BJA: 
bll2946(fadB)
BJU: 
BRA: 
BBT: 
BRS: 
S23_50670(fadB)
RPA: 
RPB: 
RPC: 
RPD: 
RPE: 
RPT: 
RPX: 
OCA: 
OCG: 
OCO: 
AOL: 
PZU: 
PHZ_c1108(fadB)
SIL: 
SPOA0285(caiD-2)
SIT: 
JAN: 
RDE: 
RD1_0613(caiD)
RLI: 
PAMI: 
PGA: 
PGL: 
PGD: 
OAT: 
OAR: 
LMD: 
SAL: 
SJP: 
SCH: 
CSH: 
RHO: 
MPA: 
MAP2645c(echA1_1)
MAO: 
MAV: 
MIT: 
MIR: 
MIA: 
MID: 
MYO: 
MSM: 
MSG: 
MSA: 
MUL: 
MUL_0972(echA1_1)
MVA: 
MGI: 
MSP: 
MMC: 
MKM: 
MJL: 
MJD: 
JDM601_1118(echA1_1)
MMI: 
MMAR_4317(echA1_1)
MRH: 
MMM: 
MCB: 
MLI: 
MULP_04515(echA1_1)
MKN: 
MNE: 
NFA: 
nfa29420(echA13)
NBR: 
ROP: 
RPY: 
GOR: 
SMA: 
SAV_1350(echA5)
SVE: 
ART: 
AAU: 
ACH: 
ARR: 
KFL: 
NDA: 
FRA: 
SEN: 
SACE_2852(caiD)
AOI: 
AORI_1505(caiD) AORI_5317(caiD)
PDX: 
EYY: 
 » show all
Taxonomy
Reference
1  [PMID:15644212]
  Authors
Koski KM, Haapalainen AM, Hiltunen JK, Glumoff T
  Title
Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzyme type 2.
  Journal
J. Mol. Biol. 345 (2005) 1157-69.
  Organism
Homo sapiens
  Sequence
[hsa:3295]
Reference
2  [PMID:9457873]
  Authors
Fukui T, Shiomi N, Doi Y
  Title
Expression and characterization of (R)-specific enoyl coenzyme A hydratase involved in polyhydroxyalkanoate biosynthesis by Aeromonas caviae.
  Journal
J. Bacteriol. 180 (1998) 667-73.
  Organism
Aeromonas caviae
  Sequence
[up:O32472]
Reference
3  [PMID:12832794]
  Authors
Koski MK, Haapalainen AM, Hiltunen JK, Glumoff T
  Title
Crystallization and preliminary crystallographic data of 2-enoyl-CoA hydratase 2  domain of Candida tropicalis peroxisomal multifunctional enzyme type 2.
  Journal
Acta. Crystallogr. D. Biol. Crystallogr. 59 (2003) 1302-5.
Reference
4  [PMID:11134939]
  Authors
Hisano T, Fukui T, Iwata T, Doi Y
  Title
Crystallization and preliminary X-ray analysis of (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis.
  Journal
Acta. Crystallogr. D. Biol. Crystallogr. 57 (2001) 145-7.
Reference
5  [PMID:16982622]
  Authors
Goepfert S, Hiltunen JK, Poirier Y
  Title
Identification and functional characterization of a monofunctional peroxisomal enoyl-CoA hydratase 2 that participates in the degradation of even cis-unsaturated fatty acids in Arabidopsis thaliana.
  Journal
J. Biol. Chem. 281 (2006) 35894-903.
  Organism
Arabidopsis thaliana
  Sequence
[ath:AT1G76150]
Reference
6  [PMID:1879422]
  Authors
Engeland K, Kindl H
  Title
Evidence for a peroxisomal fatty acid beta-oxidation involving D-3-hydroxyacyl-CoAs. Characterization of two forms of hydro-lyase that convert D-(-)-3-hydroxyacyl-CoA into 2-trans-enoyl-CoA.
  Journal
Eur. J. Biochem. 200 (1991) 171-8.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

DBGET integrated database retrieval system