KEGG   ENZYME: 1.14.19.18
Entry
EC 1.14.19.18               Enzyme                                 
Name
sphingolipid 8-(E)-desaturase;
8-sphingolipid desaturase (ambiguous);
8 fatty acid desaturase (ambiguous);
DELTA8-sphingolipid desaturase (ambiguous)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
Sysname
(4E)-sphing-4-enine ceramide,ferrocytochrome b5:oxygen oxidoreductase (8,9-trans dehydrogenating)
Reaction(IUBMB)
a (4E)-sphing-4-enine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4E,8E)-sphing-4,8-dienine ceramide + 2 ferricytochrome b5 + 2 H2O [RN:R11005]
Reaction(KEGG)
R11005
Substrate
(4E)-sphing-4-enine ceramide [CPD:C00195];
ferrocytochrome b5 [CPD:C00999];
O2 [CPD:C00007];
H+ [CPD:C00080]
Product
(4E,8E)-sphing-4,8-dienine ceramide;
ferricytochrome b5 [CPD:C00996];
H2O [CPD:C00001]
Comment
The enzyme, characterized from the yeasts Kluyveromyces lactis and Candida albicans [1] and from the diatom Thalassiosira pseudonana [2], introduces a trans double bond at the 8-position of sphingoid bases in sphingolipids. The enzyme determines the position of the double bond by its distance from the alcohol end of the sphingoid base, and contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase [3]. The homologous enzymes from higher plants, EC 1.14.19.29, sphingolipid 8-(E/Z)-desaturase, act on phytosphinganine (4-hydroxysphinganine) and produces a mixture of trans and cis isomers.
History
EC 1.14.19.18 created 2015
Orthology
K13076  sphingolipid 8-(E)-desaturase
Genes
QSU112011923 112037723
AGOAGOS_AFL079W
ERCEcym_2214
KLAKLLA0_E19471g
KMXKLMA_60375
LTHKLTH0H04488g
PPAPAS_chr1-1_0013
DHADEHA2G01628g
PICPICST_83317
PGUPGUG_00694
SPAASPAPADRAFT_140050
LELLELG_02122
CALCAALFM_C302680CA(SLD1)
CTPCTRG_02547
COTCORT_0B03390
CDUCD36_82690
CTENCANTEDRAFT_113380
YLIYALI0E21131g
CLUCLUG_02402
CLUSA9F13_24g00242
CAURCJI97_005138
SLBAWJ20_3849
PKZC5L36_0B10930
BNNFOA43_002468
BBRXBRETT_000016
OPAHPODL_00102
NCRNCU02408
NTENEUTE1DRAFT131273(NEUTE1DRAFT_131273)
SMPSMAC_08298
PANPODANSg1345 PODANSg9263
TTTTHITE_2116695
MTMMYCTH_2309213
CTHRCTHT_0048580
MGRMGG_03569
PPEIPpBr36_06705
TMNUCRPA7_1947 UCRPA7_5365
SSCKSPSK_00478 SPSK_01618
FGRFGSG_01717 FGSG_09845
FPUFPSE_11030 FPSE_11439
FVRFVEG_05080 FVEG_09818
FOXFOXG_08156 FOXG_10983
NHENECHADRAFT_103962 NECHADRAFT_30435
TRETRIREDRAFT_61367 TRIREDRAFT_65055
TRRM419DRAFT_132225 M419DRAFT_78587
MAWMAC_00112 MAC_02669 MAC_09268
MAJMAA_02135 MAA_04489 MAA_06641
CMTCCM_01221 CCM_03722 CCM_08676
PLJVFPFJ_02040 VFPFJ_02290
VALVDBG_07330 VDBG_09691
VDAVDAG_06033 VDAG_09431
CFJCFIO01_04035 CFIO01_04707
CLUPCLUP02_16126
CHIGCH63R_09566 CH63R_11900 CH63R_12449
SAPOSAPIO_CDS4535 SAPIO_CDS6496
ELAUCREL1_3375 UCREL1_9584
PFYPFICI_03505 PFICI_06520
SSLSS1G_02169 SS1G_11010
BFUBCIN_02g06380 BCIN_13g01900
MBEMBM_05993 MBM_06864
PSCOLY89DRAFT_640365 LY89DRAFT_700577
GLZGLAREA_12423
ANIAN4592.2
AFMAFUA_2G02130 AFUA_8G00590
ACTACLA_092690
NFINFIA_034500 NFIA_094040
AORAO090011000488 AO090103000137 AO090701000830
ANGANI_1_1864144(An16g06350) ANI_1_844064(An07g06770)
AFVAFLA_005340 AFLA_007873 AFLA_013381
ALUCAKAW2_11570S AKAW2_70531S
ACHEACHE_40450A
APUUAPUU_31612A APUU_70797S
PCSPc20g04400 Pc21g06390
PDPPDIP_08130 PDIP_60340
TMFPMAA_087640
TRGTRUGW13939_01822 TRUGW13939_04787
CIMCIMG_05513 CIMG_05563
CPWCPC735_066500 CPC735_066930
UREUREG_06208
PBLPAAG_03324
PBNPADG_06500
ABEARB_02524 ARB_04995
TVETRV_03106 TRV_05169
AJEHCAG_08823
BGHBDBG_05110 BDBG_06225
PNOSNOG_01379 SNOG_03145
PTEPTT_11184 PTT_16459
BZECOCCADRAFT_6350 COCCADRAFT_96002
BSCCOCSADRAFT_175963 COCSADRAFT_35049
BORCOCMIDRAFT_101558 COCMIDRAFT_79519
AALTCC77DRAFT_1022947 CC77DRAFT_1043019
ZTRMYCGRDRAFT_70915 MYCGRDRAFT_73189
PFJMYCFIDRAFT_88087
FFUCLAFUR5_09064 CLAFUR5_12145
BCOMBAUCODRAFT_34682
NPAUCRNP2_1793 UCRNP2_7036
TMLGSTUM_00007510001
CNECNB03590
CNBCNBB2110
CNGCNAG_03870
CGICGB_A2520C
TMSTREMEDRAFT_37224
TASAA1Q1_08175
PPLPOSPLDRAFT_87860
TVSTRAVEDRAFT_158995
DSQDICSQDRAFT_45749
PCOPHACADRAFT_247499
SHSSTEHIDRAFT_88813
HIRHETIRDRAFT_431762
PSQPUNSTDRAFT_58571
ADLAURDEDRAFT_111647
FMEFOMMEDRAFT_140156
GTRGLOTRDRAFT_29719
LBCLACBIDRAFT_227863
CCICC1G_10534
ABPAGABI1DRAFT110191(AGABI1DRAFT_110191)
ABVAGABI2DRAFT189913(AGABI2DRAFT_189913)
PCUBJR316_0001067
MRRMoror_17185
MOREE1B28_001016
SCMSCHCO_02487208(SCHCODRAFT_02487208)
CPUTCONPUDRAFT_115482
SLASERLADRAFT_415965 SERLADRAFT_469265
WSEWALSEDRAFT_40378
WICJ056_003600
UMAUMAG_02498
PFPPFL1_01832
MGLMGL_3864
MRTMRET_0666
MSYMMSY001_2292
PGRPGTG_07693
MLRMELLADRAFT_118135
TPSTHAPSDRAFT_22976
 » show all
Reference
1  [PMID:12402089]
  Authors
Takakuwa N, Kinoshita M, Oda Y, Ohnishi M
  Title
Isolation and characterization of the genes encoding delta(8)-sphingolipid desaturase from Saccharomyces kluyveri and Kluyveromyces lactis.
  Journal
Curr Microbiol 45:459-61 (2002)
DOI:10.1007/s00284-002-3860-0
  Sequence
Reference
2  [PMID:15978045]
  Authors
Tonon T, Sayanova O, Michaelson LV, Qing R, Harvey D, Larson TR, Li Y, Napier JA, Graham IA
  Title
Fatty acid desaturases from the microalga Thalassiosira pseudonana.
  Journal
FEBS J 272:3401-12 (2005)
DOI:10.1111/j.1742-4658.2005.04755.x
Reference
3  [PMID:19047747]
  Authors
Oura T, Kajiwara S
  Title
Disruption of the sphingolipid Delta8-desaturase gene causes a delay in morphological changes in Candida albicans.
  Journal
Microbiology 154:3795-803 (2008)
DOI:10.1099/mic.0.2008/018788-0
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.19.18
IUBMB Enzyme Nomenclature: 1.14.19.18
ExPASy - ENZYME nomenclature database: 1.14.19.18
BRENDA, the Enzyme Database: 1.14.19.18

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