KEGG   ENZYME: 1.2.1.95
Entry
EC 1.2.1.95                 Enzyme                                 
Name
L-2-aminoadipate reductase;
LYS2;
alpha-aminoadipate reductase
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
Sysname
(S)-2-amino-6-oxohexanoate:NADP+ oxidoreductase (ATP-forming)
Reaction(IUBMB)
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate = L-2-aminoadipate + NADPH + H+ + ATP (overall reaction) [RN:R11679];
(1a) L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + AMP + diphosphate = L-2-aminoadipate + holo-[LYS2 peptidyl-carrier-protein] + ATP;
(1b) (S)-2-amino-6-oxohexanoate + holo-[LYS2 peptidyl-carrier-protein] + NADP+ = L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + NADPH + H+
Reaction(KEGG)
R11679;
(other) R03098 R04390 R04863
Substrate
(S)-2-amino-6-oxohexanoate [CPD:C04076];
NADP+ [CPD:C00006];
AMP [CPD:C00020];
diphosphate [CPD:C00013];
L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein];
holo-[LYS2 peptidyl-carrier-protein]
Product
L-2-aminoadipate [CPD:C00956];
NADPH [CPD:C00005];
H+ [CPD:C00080];
ATP [CPD:C00002];
holo-[LYS2 peptidyl-carrier-protein];
L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein]
Comment
This enzyme, characterized from the yeast Saccharomyces cerevisiae, catalyses the reduction of L-2-aminoadipate to (S)-2-amino-6-oxohexanoate during L-lysine biosynthesis. An adenylation domain activates the substrate at the expense of ATP hydrolysis, and forms L-2-aminoadipate adenylate, which is attached to a peptidyl-carrier protein (PCP) domain. Binding of NADPH results in reductive cleavage of the acyl-S-enzyme intermediate, releasing (S)-2-amino-6-oxohexanoate. Different from EC 1.2.1.31, L-aminoadipate-semialdehyde dehydrogenase, which catalyses a similar transformation in the opposite direction without ATP hydrolysis.
History
EC 1.2.1.95 created 2015
Pathway
ec00300  Lysine biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K00143  L-2-aminoadipate reductase
Genes
QSU112018202 112040294
SCEYBR115C(LYS2)
AGOAGOS_ADL346W
ERCEcym_3457
KLAKLLA0_B09218g
KMXKLMA_80299(LYS2)
LTHKLTH0F10384g
VPOKpol_1006p6
ZROZYRO0C16566g
CGRCAGL0K07788g
NCSNCAS_0I01040(NCAS0I01040)
NDINDAI_0A07970(NDAI0A07970)
TPFTPHA_0A03520(TPHA0A03520)
TBLTBLA_0H01500(TBLA0H01500)
TDLTDEL_0C05110(TDEL0C05110)
TGBHG536_0B02090
KAFKAFR_0D02630(KAFR0D02630)
ZMKHG535_0A02150
PPAPAS_chr1-4_0153
DHADEHA2D07964g
PICPICST_68020(LYS2)
PGUPGUG_04759
SPAASPAPADRAFT_145301(LYS2)
LELLELG_01517
CALCAALFM_C102820WA(LYS2)
CTPCTRG_04682
COTCORT_0B09490
CDUCD36_02620
CTENCANTEDRAFT_131638
YLIYALI0E06457g
CLUCLUG_04446
CLUSA9F13_04g00583
CAURCJI97_003346
SLBAWJ20_3018(LYS2)
PKZC5L36_0B12020
BNNFOA43_003074
BBRXBRETT_005327
NCRNCU03010(lys-3)
NTENEUTE1DRAFT126732(NEUTE1DRAFT_126732)
SMPSMAC_01210
PANPODANSg09765
TTTTHITE_2122221
MTMMYCTH_2295392
CTHRCTHT_0055440
MGRMGG_02611
TMNUCRPA7_7828
SSCKSPSK_02958
FGRFGSG_06041
FPUFPSE_02931
FVRFVEG_08245
FOXFOXG_01867 FOXG_11115
NHENECHADRAFT_76435(NhLYS2) NECHADRAFT_81329
TRETRIREDRAFT_4117
TRRM419DRAFT_67857
MAWMAC_09675
MAJMAA_03758
CMTCCM_03390
PLJVFPFJ_09219
VALVDBG_05463
VDAVDAG_07112
CFJCFIO01_05721
SAPOSAPIO_CDS6728 SAPIO_CDS9122
ELAUCREL1_11578
PFYPFICI_11756
SSLSS1G_08185
BFUBCIN_04g00140(Bclys2)
MBEMBM_08979
PSCOLY89DRAFT_784917
GLZGLAREA_03383
ANIAN5610.2
AFMAFUA_4G11240
ACTACLA_050330
NFINFIA_105160
AORAO090003001097
ANGANI_1_1902184(An04g05420)
AFVAFLA_000572
ALUCAKAW2_51512A(LYS2)
ACHEACHE_40446S(LYS2_2)
APUUAPUU_40975S(LYS2)
PCSPc22g06310(Lys2)
PDPPDIP_33720
TMFPMAA_020860
TRGTRUGW13939_04324
CIMCIMG_01491
CPWCPC735_049520
UREUREG_05106
PBLPAAG_08023
PBNPADG_08092
ABEARB_02279
TVETRV_04974
AJEHCAG_09107
BGHBDBG_06043
PNOSNOG_07784
PTEPTT_09387
BZECOCCADRAFT_321
BSCCOCSADRAFT_105593(AAR)
BORCOCMIDRAFT_912
AALTCC77DRAFT_1016196
ZTRMYCGRDRAFT_99148(LYS2)
PFJMYCFIDRAFT_46827
BCOMBAUCODRAFT_263156
NPAUCRNP2_5911
TMLGSTUM_00010502001
SPOSPAP7G5.04c(lys1)
CNECNG00170
CNBCNBG4570
CGICGB_G6500C
TMSTREMEDRAFT_44814
TASAA1Q1_01219
TVSTRAVEDRAFT_171224
DSQDICSQDRAFT_101950
PCOPHACADRAFT_118411
SHSSTEHIDRAFT_85460
HIRHETIRDRAFT_66316(lys2)
PSQPUNSTDRAFT_102428
ADLAURDEDRAFT_110234
FMEFOMMEDRAFT_118412
GTRGLOTRDRAFT_78681
LBCLACBIDRAFT_184376(LbLYS1)
MRRMoror_9060
CCICC1G_15694
SCMSCHCODRAFT_59997
ABPAGABI1DRAFT79561(AGABI1DRAFT_79561)
ABVAGABI2DRAFT208996(AGABI2DRAFT_208996)
CPUTCONPUDRAFT_168209
SLASERLADRAFT_359475
WSEWALSEDRAFT_22743
WICJ056_002659
UMAUMAG_01697
PFPPFL1_03572
MGLMGL_0235
MRTMRET_1079
MSYMMSY001_3374
PGRPGTG_07683
MLRMELLADRAFT_54227
SREPTSG_11594
ACANACA1_063720
NGRNAEGRDRAFT_77825
 » show all
Reference
1  [PMID:10320345]
  Authors
Ehmann DE, Gehring AM, Walsh CT
  Title
Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5.
  Journal
Biochemistry 38:6171-7 (1999)
DOI:10.1021/bi9829940
  Sequence
[sce:YBR115C]
Other DBs
ExplorEnz - The Enzyme Database: 1.2.1.95
IUBMB Enzyme Nomenclature: 1.2.1.95
ExPASy - ENZYME nomenclature database: 1.2.1.95
BRENDA, the Enzyme Database: 1.2.1.95
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