Entry
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
SHR : 100931196 100931457 100931720
CABI : 116830887 116837371
SRX : 107717245(ephx2) 107733988
SANH : 107653762 107692411
SGH : 107552031 107594076(ephx2)
CAUA : 113060837 113117731
CGIB : 127976311 128031809
RKG : 130088847 130088950(ephx2)
MSAM : 119892822 119901244 119901687 119901935 119903463 119915610
ALAT : 119015231 119015235
SASA : 106604359(HYES) 106611412(HYES)
STRU : 115161918 115172954
OTW : 112239012 112239182 112256950
OMY : 110498218(ephx2) 110504256
OGO : 124001944(ephx2) 124046757
OKE : 118380841 127913538(ephx2)
CCLU : 121539061(ephx2) 121544563
SCLV : 120337441 120337631
SPU : 590472(EH1) 752510(eh2)
LPIC : 129260275 129261305 129261533
APLC : 110985936 110985937
TAD : TRIADDRAFT_30313 TRIADDRAFT_59995 TRIADDRAFT_60010 TRIADDRAFT_60079 TRIADDRAFT_64238
YLI : YALI0C23224g YALI0E19899g
NTE : NEUTE1DRAFT119163(NEUTE1DRAFT_119163)
SMP : SMAC_06471 SMAC_12126
PAN : PODANSg2586 PODANSg4881
MGR : MGG_05175 MGG_05826 MGG_07954 MGG_09603 MGG_13875
FGR : FGSG_06744 FGSG_11196
FPU : FPSE_02822 FPSE_09090
FOX : FOXG_08935 FOXG_10109 FOXG_13323 FOXG_14841 FOXG_19442 FOXG_22390
NHE : NECHADRAFT_30431 NECHADRAFT_38604 NECHADRAFT_51532 NECHADRAFT_98121
TRE : TRIREDRAFT_53220 TRIREDRAFT_57045
TRR : M419DRAFT_69084 M419DRAFT_72359
VAL : VDBG_05347 VDBG_08907
VDA : VDAG_06569 VDAG_06997
CFJ : CFIO01_01948 CFIO01_02421 CFIO01_04356 CFIO01_06499 CFIO01_11995
CHIG : CH63R_09605 CH63R_12939
ELA : UCREL1_10468 UCREL1_2213 UCREL1_3351 UCREL1_9854
PFY : PFICI_03331 PFICI_05569 PFICI_08381 PFICI_14790
SSL : SS1G_08093 SS1G_13652
BFU : BCIN_10g01840 BCIN_13g00770 BCIN_15g00230
PSCO : LY89DRAFT_507394 LY89DRAFT_594279 LY89DRAFT_662388 LY89DRAFT_683181 LY89DRAFT_702826 LY89DRAFT_785580
GLZ : GLAREA_02712 GLAREA_04148 GLAREA_09895 GLAREA_12612
TRG : TRUGW13939_04437 TRUGW13939_05195 TRUGW13939_08349
AJE : HCAG_03262 HCAG_06274
PNO : SNOG_12792 SNOG_13782(SNOG_13781) SNOG_14994
BZE : COCCADRAFT_10479 COCCADRAFT_23112 COCCADRAFT_24314
BSC : COCSADRAFT_329080 COCSADRAFT_37209
BOR : COCMIDRAFT_26566 COCMIDRAFT_3129 COCMIDRAFT_97004
AALT : CC77DRAFT_1020259 CC77DRAFT_1067778 CC77DRAFT_23691 CC77DRAFT_924398 CC77DRAFT_933869 CC77DRAFT_991934
ZTR : MYCGRDRAFT_101398 MYCGRDRAFT_45185 MYCGRDRAFT_67922 MYCGRDRAFT_69862 MYCGRDRAFT_74004
PFJ : MYCFIDRAFT_186960 MYCFIDRAFT_202874 MYCFIDRAFT_31012 MYCFIDRAFT_35544 MYCFIDRAFT_63852
NPA : UCRNP2_1253 UCRNP2_2402 UCRNP2_2781 UCRNP2_536 UCRNP2_578 UCRNP2_7692 UCRNP2_9159
TVS : TRAVEDRAFT_114934 TRAVEDRAFT_116461 TRAVEDRAFT_121619 TRAVEDRAFT_163026 TRAVEDRAFT_171945 TRAVEDRAFT_42938 TRAVEDRAFT_42939 TRAVEDRAFT_42940 TRAVEDRAFT_42941 TRAVEDRAFT_42942 TRAVEDRAFT_60092 TRAVEDRAFT_72850 TRAVEDRAFT_94256
DSQ : DICSQDRAFT_101446 DICSQDRAFT_104823 DICSQDRAFT_61223
PCO : PHACADRAFT_104575 PHACADRAFT_118086 PHACADRAFT_151144 PHACADRAFT_191247 PHACADRAFT_194943 PHACADRAFT_198096 PHACADRAFT_207661 PHACADRAFT_208465 PHACADRAFT_255121 PHACADRAFT_260148 PHACADRAFT_91351 PHACADRAFT_93100
SHS : STEHIDRAFT_106361 STEHIDRAFT_122857 STEHIDRAFT_61089 STEHIDRAFT_80676 STEHIDRAFT_81610
HIR : HETIRDRAFT_148090 HETIRDRAFT_155125 HETIRDRAFT_156748 HETIRDRAFT_156749 HETIRDRAFT_174637 HETIRDRAFT_63479
PSQ : PUNSTDRAFT_112781 PUNSTDRAFT_116520 PUNSTDRAFT_139547 PUNSTDRAFT_98990
ADL : AURDEDRAFT_110586 AURDEDRAFT_117379 AURDEDRAFT_117569 AURDEDRAFT_117572 AURDEDRAFT_152313 AURDEDRAFT_175477 AURDEDRAFT_80706
FME : FOMMEDRAFT_106649 FOMMEDRAFT_127219 FOMMEDRAFT_135095
GTR : GLOTRDRAFT_45684 GLOTRDRAFT_68350
RSX : RhiXN_03509 RhiXN_04225 RhiXN_05233 RhiXN_07686
LBC : LACBIDRAFT_303899 LACBIDRAFT_311540(LbEPHX1)
CCI : CC1G_00644 CC1G_00645 CC1G_14690
ABP : AGABI1DRAFT110229(AGABI1DRAFT_110229) AGABI1DRAFT38499(AGABI1DRAFT_38499) AGABI1DRAFT70817(AGABI1DRAFT_70817)
ABV : AGABI2DRAFT184905(AGABI2DRAFT_184905) AGABI2DRAFT189875(AGABI2DRAFT_189875) AGABI2DRAFT78715(AGABI2DRAFT_78715)
MPR : MPER_04928 MPER_09275 MPER_11089
MRR : Moror_11208 Moror_13472 Moror_13512 Moror_13860 Moror_14385 Moror_14388 Moror_16097 Moror_2330 Moror_2947 Moror_4070 Moror_6712 Moror_8127
MORE : E1B28_004695 E1B28_008290
SCM : SCHCO_01159789(SCHCODRAFT_01159789) SCHCO_02625205(SCHCODRAFT_02625205) SCHCO_02645722(SCHCODRAFT_02645722) SCHCO_02666784(SCHCODRAFT_02666784)
CPUT : CONPUDRAFT_122227 CONPUDRAFT_93019
SLA : SERLADRAFT_354546 SERLADRAFT_448219 SERLADRAFT_479064 SERLADRAFT_479070 SERLADRAFT_480679
PGR : PGTG_00491 PGTG_05962 PGTG_05973
MLR : MELLADRAFT_102079 MELLADRAFT_115158 MELLADRAFT_123933
PIF : PITG_11920 PITG_11921 PITG_11922 PITG_15955 PITG_15956
PSOJ : PHYSODRAFT_314147 PHYSODRAFT_318677 PHYSODRAFT_525117 PHYSODRAFT_558062 PHYSODRAFT_564652
SPAR : SPRG_06039 SPRG_06040 SPRG_06041
» show all
Taxonomy
Reference
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
Sequence
Reference
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
Reference
Authors
Morisseau C, Hammock BD.
Title
Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles.
Journal
Reference
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
Reference
Authors
Newman JW, Morisseau C, Hammock BD.
Title
Epoxide hydrolases: their roles and interactions with lipid metabolism.
Journal
Sequence
Reference
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
Reference
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
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.1.3.76
ExPASy - ENZYME nomenclature database: 3.1.3.76