KEGG   ENZYME: 3.1.3.76Help
Entry
EC 3.1.3.76                 Enzyme                                 

Name
lipid-phosphate phosphatase;
hydroxy fatty acid phosphatase;
dihydroxy fatty acid phosphatase;
hydroxy lipid phosphatase;
sEH (ambiguous);
soluble epoxide hydrolase (ambiguous)
Class
Hydrolases;
Acting on ester bonds;
Phosphoric-monoester hydrolases
BRITE hierarchy
Sysname
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate phosphohydrolase
Reaction(IUBMB)
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate [RN:R07582]
Reaction(KEGG)
Substrate
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate [CPD:C15989];
H2O [CPD:C00001]
Product
(9S,10S)-9,10-dihydroxyoctadecanoate [CPD:C15988];
phosphate [CPD:C00009]
Comment
Requires Mg2+ for maximal activity. The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10, soluble epoxide hydrolase (sEH) [1]. The best substrates for this enzyme are 10-hydroxy-9-(phosphonooxy)octadecanoates, with the threo- form being a better substrate than the erythro- form [1]. The phosphatase activity is not found in plant sEH or in EC 3.3.2.9, microsomal epoxide hydrolase, from mammals [1].
History
EC 3.1.3.76 created 2006
Orthology
K08726  
soluble epoxide hydrolase / lipid-phosphate phosphatase
Genes
HSA: 
2053(EPHX2)
PTR: 
464074(EPHX2)
PPS: 
100990932(EPHX2)
GGO: 
101136750(EPHX2)
PON: 
100172736(EPHX2)
NLE: 
100585861(EPHX2)
MCC: 
712926(EPHX2)
MCF: 
102134633(EPHX2)
RRO: 
104673945(EPHX2)
CJC: 
100402999(EPHX2)
MMU: 
13850(Ephx2)
RNO: 
65030(Ephx2)
CGE: 
100757328(Ephx2)
NGI: 
103730002(Ephx2)
HGL: 
101715352(Ephx2)
OCU: 
100350230(EPHX2)
TUP: 
102480725(EPHX2)
CFA: 
477373(EPHX2)
AML: 
100483572(EPHX2)
UMR: 
103675990(EPHX2)
FCA: 
101092355(EPHX2)
PTG: 
102957184(EPHX2)
BTA: 
511716(EPHX2)
BOM: 
102267808(EPHX2)
PHD: 
102326909(EPHX2)
CHX: 
102185835(EPHX2)
OAS: 
101106654(EPHX2)
SSC: 
414425(EPHX2)
CFR: 
102517269(EPHX2)
BACU: 
103015729(EPHX2)
LVE: 
103082628(EPHX2)
ECB: 
100060414(EPHX2)
MYB: 
102255588(EPHX2)
MYD: 
102755564(EPHX2)
PALE: 
102886924(EPHX2)
MDO: 
100030580(EPHX2)
SHR: 
OAA: 
100093187(EPHX2)
GGA: 
421999(EPHX2)
MGP: 
100550075(EPHX2)
CJO: 
107312419(EPHX2)
APLA: 
101802271(EPHX2)
FAB: 
101820851(EPHX2)
PHI: 
102113903(EPHX2)
CCW: 
104686792(EPHX2)
FPG: 
101922601(EPHX2)
FCH: 
102047869(EPHX2)
CLV: 
102084991(EPHX2)
AAM: 
106486373(EPHX2)
ASN: 
102382847(EPHX2)
AMJ: 
102558789(EPHX2)
PSS: 
102463793(EPHX2)
CMY: 
102944771(EPHX2)
ACS: 
100564154(ephx2)
PBI: 
GJA: 
107118053(EPHX2)
XLA: 
447032(ephx2)
XTR: 
448759(ephx2)
DRE: 
494099(ephx2)
TRU: 
101078765(ephx2)
MZE: 
101483599(ephx2)
OLA: 
101157276(ephx2)
XMA: 
102235090(ephx2)
BFO: 
CIN: 
SPU: 
590376 590472(EH1) 752510(eh2)
SKO: 
NVE: 
TAD: 
CIC: 
PXB: 
CMO: 
YLI: 
NCR: 
MGR: 
PNO: 
PTE: 
PFJ: 
DSQ: 
PCO: 
SHS: 
HIR: 
PSQ: 
ADL: 
FME: 
LBC: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT38499(AGABI1DRAFT_38499) AGABI1DRAFT70817(AGABI1DRAFT_70817)
ABV: 
AGABI2DRAFT78715(AGABI2DRAFT_78715)
CPUT: 
SLA: 
WSE: 
WIC: 
UMA: 
PFP: 
PGR: 
MLR: 
ACAN: 
PIF: 
PSOJ: 
SPAR: 
 » show all
Taxonomy
Reference
1  [PMID:12574510]
  Authors
Newman JW, Morisseau C, Harris TR, Hammock BD.
  Title
The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 1558-63.
  Sequence
[hsa:2053]
Reference
2  [PMID:12574508]
  Authors
Cronin A, Mowbray S, Durk H, Homburg S, Fleming I, Fisslthaler B, Oesch F, Arand M.
  Title
The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 1552-7.
Reference
3  [PMID:15822179]
  Authors
Morisseau C, Hammock BD.
  Title
Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles.
  Journal
Annu. Rev. Pharmacol. Toxicol. 45 (2005) 311-33.
Reference
4  [PMID:16142916]
  Authors
Tran KL, Aronov PA, Tanaka H, Newman JW, Hammock BD, Morisseau C.
  Title
Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble epoxide hydrolase.
  Journal
Biochemistry. 44 (2005) 12179-87.
Reference
5  [PMID:15748653]
  Authors
Newman JW, Morisseau C, Hammock BD.
  Title
Epoxide hydrolases: their roles and interactions with lipid metabolism.
  Journal
Prog. Lipid. Res. 44 (2005) 1-51.
  Sequence
[hsa:2053]
Reference
6  [PMID:15196990]
  Authors
Srivastava PK, Sharma VK, Kalonia DS, Grant DF.
  Title
Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure.
  Journal
Arch. Biochem. Biophys. 427 (2004) 164-9.
Reference
7  [PMID:15096040]
  Authors
Gomez GA, Morisseau C, Hammock BD, Christianson DW.
  Title
Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis.
  Journal
Biochemistry. 43 (2004) 4716-23.
  Sequence
[hsa:2053]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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