T00219
type: Enzyme
cath: Rossmann fold
cath: Dihydrodipicolinate Reductase; domain 2
cath: Domain 3, Saccharopine reductase
ec: https://purl.uniprot.org/enzyme/1.5.1.10
csa: 1e5q
uniprot: Q9P4R4
kegg enzyme: saccharopine dehydrogenase (NADP+, L-glutamate-forming)
kegg enzyme: saccharopine (nicotinamide adenine dinucleotide phosphate,glutamate-forming) dehydrogenase
kegg enzyme: aminoadipic semialdehyde-glutamic reductase
kegg enzyme: aminoadipate semialdehyde-glutamate reductase
kegg enzyme: aminoadipic semialdehyde-glutamate reductase
kegg enzyme: epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase(L-2-aminoadipate-semialdehyde forming)
kegg enzyme: saccharopine reductase
kegg enzyme: 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase(L-glutamate-forming)
kegg pathway: Lysine biosynthesis
kegg pathway: Lysine degradation
kegg substrate: NADPH
kegg substrate: L-Glutamate
kegg substrate: L-2-Aminoadipate 6-semialdehyde
kegg substrate: H+
kegg product: NADP+
kegg product: N6-(L-1,3-Dicarboxypropyl)-L-lysine
kegg product: H2O
pdb: 1e5lA01
pdb: 1e5lB01
pdb: 1e5qA01
pdb: 1e5qB01
pdb: 1e5qC01
pdb: 1e5qD01
pdb: 1e5qE01
pdb: 1e5qF01
pdb: 1e5qG01
pdb: 1e5qH01
pdb: 1ff9A01
pdb: 1e5lA02
pdb: 1e5lB02
pdb: 1e5qA02
pdb: 1e5qB02
pdb: 1e5qC02
pdb: 1e5qD02
pdb: 1e5qE02
pdb: 1e5qF02
pdb: 1e5qG02
pdb: 1e5qH02
pdb: 1ff9A02
pdb: 1e5lA03
pdb: 1e5lB03
pdb: 1e5qA03
pdb: 1e5qB03
pdb: 1e5qC03
pdb: 1e5qD03
pdb: 1e5qE03
pdb: 1e5qF03
pdb: 1e5qG03
pdb: 1e5qH03
pdb: 1ff9A03
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5lA01
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5lB01
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5qA01
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5qB01
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5qC01
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5qD01
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5qE01
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5qF01
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5qG01
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5qH01
pdb bound state: Unbound
  compound: NADPH
  pdb: 1ff9A01
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5lA02
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5lB02
pdb bound state: Unbound
  compound: NADPH
  pdb: 1ff9A02
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5lA03
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5lB03
pdb bound state: Unbound
  compound: NADPH
  pdb: 1e5qA03
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/T00219#4
references: Properties of partially purified saccharopine dehydrogenase from human placenta.
references: Phylogenetic analyses of proton-translocating transhydrogenases.
references: Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/T00219#4
comment: Saccharopine Dehydrogenases are a collective term for the enzymes that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-lysine, or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-glutamate. According to the paper [3], this enzyme catalyzes three different reactions, addition to double-bond, elimination accompanied by double-bond formation, and reduction.

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720

Dihydrodipicolinate Reductase; domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.360.10
catalytic domain: index.html

Domain 3, Saccharopine reductase
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.1870.10

Lysine biosynthesis
type: KeggPathway
references: KEGG:MAP00300

Lysine degradation
type: KeggPathway
references: KEGG:MAP00310

NADPH
type: KeggSubstrate
references: KEGG:C00005
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16474
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Glutamate
type: KeggSubstrate
references: KEGG:C00025
compound type: amino acids
compound type: carboxyl group
references: CHEBI:16015
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-2-Aminoadipate 6-semialdehyde
type: KeggSubstrate
references: KEGG:C04076
compound type: amino acids
compound type: carbohydrate
compound type: lipid
references: CHEBI:17917
references: CHEBI:58321
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H+
type: KeggSubstrate
references: KEGG:C00080
compound type: others
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADP+
type: KeggProduct
references: KEGG:C00006
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:18009
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

N6-(L-1,3-Dicarboxypropyl)-L-lysine
type: KeggProduct
references: KEGG:C00449
compound type: amino acids
compound type: amine group
compound type: carboxyl group
references: CHEBI:16927
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H2O
type: KeggProduct
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1e5lA02
type: Pdb
references: 1e5l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5l
catalytic residue: ASP 126

1e5lB02
type: Pdb
references: 1e5l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5l
catalytic residue: ASP 126

1e5qA02
type: Pdb
references: 1e5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5q
catalytic residue: ASP 126

1e5qB02
type: Pdb
references: 1e5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5q
catalytic residue: ASP 126

1e5qC02
type: Pdb
references: 1e5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5q
catalytic residue: ASP 126

1e5qD02
type: Pdb
references: 1e5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5q
catalytic residue: ASP 126

1e5qE02
type: Pdb
references: 1e5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5q
catalytic residue: ASP 126

1e5qF02
type: Pdb
references: 1e5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5q
catalytic residue: ASP 126

1e5qG02
type: Pdb
references: 1e5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5q
catalytic residue: ASP 126

1e5qH02
type: Pdb
references: 1e5q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5q
catalytic residue: ASP 126

1ff9A02
type: Pdb
references: 1ff9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ff9
catalytic residue: ASP 126

Properties of partially purified saccharopine dehydrogenase from human placenta.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/242268
journal: Arch Biochem Biophys
volume: 171
pages: 191-6
published year: 1975
authors:
  item: Fjellstedt TA
  item: Robinson JC

Phylogenetic analyses of proton-translocating transhydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10587945
journal: Microb Comp Genomics
volume: 4
pages: 173-86
published year: 1999
authors:
  item: Studley WK
  item: Yamaguchi M
  item: Hatefi Y
  item: Saier MH Jr

Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11080625
journal: Structure Fold Des
volume: 8
pages: 1037-47
published year: 2000
authors:
  item: Johansson E
  item: Steffens JJ
  item: Lindqvist Y
  item: Schneider G
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00219#4
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12393892
journal: J Biol Chem
volume: 277
pages: 49655-61
published year: 2002
authors:
  item: Zhu X
  item: Tang G
  item: Galili G
title: The activity of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is regulated by functional interaction between its two enzyme domains.

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.7, p.1042-1044
reference step: 3