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
Lysine biosynthesis
Metabolic pathways
Orthology
K00143  
L-2-aminoadipate reductase
Genes
SCE: 
YBR115C(LYS2)
AGO: 
ERC: 
KLA: 
LTH: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0I01040(NCAS0I01040)
NDI: 
NDAI_0A07970(NDAI0A07970)
TPF: 
TPHA_0A03520(TPHA0A03520)
TBL: 
TBLA_0H01500(TBLA0H01500)
TDL: 
TDEL_0C05110(TDEL0C05110)
KAF: 
KAFR_0D02630(KAFR0D02630)
PPA: 
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CTP: 
COT: 
CDU: 
CTEN: 
YLI: 
CLU: 
CAUR: 
NCR: 
NCU03010(lys-3)
NTE: 
NEUTE1DRAFT126732(NEUTE1DRAFT_126732)
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
FPU: 
FVR: 
FOX: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
PLJ: 
VAL: 
VDA: 
CFJ: 
ELA: 
PFY: 
SSL: 
BFU: 
MBE: 
PSCO: 
GLZ: 
ANI: 
AFM: 
AOR: 
AOR_1_1954154(AO090003001097)
ANG: 
ANI_1_1902184(An04g05420)
AFV: 
ACT: 
NFI: 
PCS: 
PDP: 
CIM: 
CPW: 
PBL: 
PBN: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
TMS: 
TVS: 
DSQ: 
PCO: 
SHS: 
HIR: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MPR: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT79561(AGABI1DRAFT_79561)
ABV: 
AGABI2DRAFT208996(AGABI2DRAFT_208996)
CPUT: 
SLA: 
WSE: 
WIC: 
UMA: 
PFP: 
MGL: 
PGR: 
MLR: 
MBR: 
SRE: 
DPP: 
ACAN: 
NGR: 
NGV: 
 » 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: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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