KEGG   ENZYME: 1.2.1.95Help
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
BRITE hierarchy
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)
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
Orthology
K00143  L-2-aminoadipate reductase
Genes
SCE: YBR115C(LYS2)
AGO: AGOS_ADL346W
ERC: Ecym_3457
KLA: KLLA0B09218g
KMX: KLMA_80299(LYS2)
LTH: KLTH0F10384g
VPO: Kpol_1006p6
ZRO: ZYRO0C16566g
CGR: CAGL0K07788g
NCS: NCAS_0I01040(NCAS0I01040)
NDI: NDAI_0A07970(NDAI0A07970)
TPF: TPHA_0A03520(TPHA0A03520)
TBL: TBLA_0H01500(TBLA0H01500)
TDL: TDEL_0C05110(TDEL0C05110)
KAF: KAFR_0D02630(KAFR0D02630)
PIC: PICST_68020(LYS2)
SPAA: SPAPADRAFT_145301(LYS2)
CAL: CAALFM_C102820WA(LYS2)
CAUR: QG37_02011
SLB: AWJ20_3018(LYS2)
NCR: NCU03010(lys-3)
NTE: NEUTE1DRAFT126732(NEUTE1DRAFT_126732)
MGR: MGG_02611
MAW: MAC_09675
CMT: CCM_03390
MBE: MBM_08979
ANI: AN5610.2
ANG: ANI_1_1902184(An04g05420)
PCS: Pc22g06310(Lys2)
ABE: ARB_02279
TVE: TRV_04974
PTE: PTT_09387
ZTR: MYCGRDRAFT_99148(LYS2)
SPO: SPAP7G5.04c(lys1)
CNE: CNG00170
CNB: CNBG4570
HIR: HETIRDRAFT_66316(lys2)
LBC: LACBIDRAFT_184376(LbLYS1)
ABP: AGABI1DRAFT79561(AGABI1DRAFT_79561)
ABV: AGABI2DRAFT208996(AGABI2DRAFT_208996)
MGL: MGL_0235
 » show all
Taxonomy
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 (1999) 6171-7.
  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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