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);
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate phosphohydrolase
Class
Hydrolases;
Acting on ester bonds;
Phosphoric-monoester hydrolases
BRITE hierarchy
Sysname
(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate phosphohydrolase
Reaction(IUBMB)
(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate [RN:R07582]
Reaction(KEGG)
Substrate
(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate;
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-(phosphooxy)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)
CSAB: 103215526(EPHX2)
RRO: 104673945(EPHX2)
RBB: 108537568(EPHX2)
CJC: 100402999(EPHX2)
SBQ: 101033420(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)
ORO: 101373863(EPHX2)
FCA: 101092355(EPHX2)
PTG: 102957184(EPHX2)
AJU: 106973110(EPHX2)
BTA: 511716(EPHX2)
BOM: 102267808(EPHX2)
BIU: 109563159(EPHX2)
PHD: 102326909(EPHX2)
CHX: 102185835(EPHX2)
OAS: 101106654(EPHX2)
SSC: 414425(EPHX2)
CFR: 102517269(EPHX2)
CDK: 105102229(EPHX2)
BACU: 103015729(EPHX2)
LVE: 103082628(EPHX2)
OOR: 101282222(EPHX2)
ECB: 100060414(EPHX2)
EPZ: 103550424(EPHX2)
EAI: 106832514(EPHX2)
MYB: 102255588(EPHX2)
MYD: 102755564(EPHX2)
HAI: 109379561(EPHX2)
RSS: 109448144(EPHX2)
PALE: 102886924(EPHX2)
LAV: 100658579(EPHX2)
TMU: 101343713
MDO: 100030580(EPHX2)
OAA: 100093187(EPHX2)
GGA: 421999(EPHX2)
MGP: 100550075(EPHX2)
CJO: 107312419(EPHX2)
APLA: 101802271(EPHX2)
ACYG: 106049519(EPHX2)
FAB: 101820851(EPHX2)
PHI: 102113903(EPHX2)
CCAE: 111927478(EPHX2) 111945878
FPG: 101922601(EPHX2)
FCH: 102047869(EPHX2)
CLV: 102084991(EPHX2)
EGZ: 104132029(EPHX2)
AAM: 106486373(EPHX2)
ASN: 102382847(EPHX2)
AMJ: 102558789(EPHX2)
PSS: 102463793(EPHX2)
CMY: 102944771(EPHX2)
ACS: 100564154(ephx2)
PVT: 110089501(EPHX2)
GJA: 107118053(EPHX2)
XLA: 447032(ephx2.L)
XTR: 448759(ephx2)
NPR: 108798538(EPHX2)
DRE: 494099(ephx2)
SRX: 107717245(ephx2) 107733988
SGH: 107552031 107594076(ephx2)
IPU: 108270338(ephx2)
AMEX: 103037948(ephx2)
TRU: 101078765(ephx2)
LCO: 104928568(ephx2)
NCC: 104958265(ephx2)
MZE: 101483599(ephx2)
OLA: 101157276(ephx2)
XMA: 102235090(ephx2)
PRET: 103456621(ephx2)
NFU: 107384625(ephx2)
KMR: 108246829(ephx2)
LCF: 108873166(ephx2) 108879368
SDU: 111234755(ephx2)
MALB: 109955803(ephx2)
SASA: 106604359(HYES) 106611412(HYES)
ELS: 105028738(ephx2)
SPU: 590376 590472(EH1) 752510(eh2)
EPA: 110251610
AQU: 105313986
DZI: 111281598
PXB: 103939771
NTA: 107766629
NTO: 108948202
NCR: NCU02924
MGR: MGG_05826
PTE: PTT_13711
ABP: AGABI1DRAFT38499(AGABI1DRAFT_38499) AGABI1DRAFT70817(AGABI1DRAFT_70817)
ABV: AGABI2DRAFT78715(AGABI2DRAFT_78715)
 » 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 100:1558-63 (2003)
DOI:10.1073/pnas.0437724100
  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 100:1552-7 (2003)
DOI:10.1073/pnas.0437829100
Reference
3  [PMID:15822179]
  Authors
Morisseau C, Hammock BD.
  Title
Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles.
  Journal
Annu Rev Pharmacol Toxicol 45:311-33 (2005)
DOI:10.1146/annurev.pharmtox.45.120403.095920
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 44:12179-87 (2005)
DOI:10.1021/bi050842g
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 44:1-51 (2005)
DOI:10.1016/j.plipres.2004.10.001
  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 427:164-9 (2004)
DOI:10.1016/j.abb.2004.05.003
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 43:4716-23 (2004)
DOI:10.1021/bi036189j
  Sequence
[hsa:2053]
Other DBs
ExplorEnz - The Enzyme Database: 3.1.3.76
IUBMB Enzyme Nomenclature: 3.1.3.76
ExPASy - ENZYME nomenclature database: 3.1.3.76
BRENDA, the Enzyme Database: 3.1.3.76

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