D00840
type: Enzyme
cath: Rossmann fold
cath: Dehydroquinate synthase-like, alpha domain
ec: https://purl.uniprot.org/enzyme/1.1.1.77
uniprot: P0A9S1
kegg enzyme: Lactaldehyde reductase
kegg enzyme: Propanediol:nicotinamide adenine dinucleotide (NAD+) oxidoreductase
kegg enzyme: L-Lactaldehyde:propanediol oxidoreductase
kegg pathway: Pyruvate metabolism
kegg pathway: Glyoxylate and dicarboxylate metabolism
kegg cofactor: Iron
kegg substrate: (R)-propane-1,2-diol
kegg substrate: (S)-propane-1,2-diol
kegg substrate: NAD+
kegg product: (R)-lactaldehyde
kegg product: (S)-lactaldehyde
kegg product: NADH
kegg product: H+
pdb: 1rrmA01
pdb: 1rrmB01
pdb: 2bi4A01
pdb: 2bi4B01
pdb: 2bl4A01
pdb: 2bl4B01
pdb: 1rrmA02
pdb: 1rrmB02
pdb: 2bi4A02
pdb: 2bi4B02
pdb: 2bl4A02
pdb: 2bl4B02
pdb bound state: Unbound
  compound: (R)-propane-1,2-diol
  pdb: 1rrmA01
pdb bound state: Unbound
  compound: (R)-propane-1,2-diol
  pdb: 1rrmB01
pdb bound state: Unbound
  compound: (R)-propane-1,2-diol
  pdb: 2bi4A01
pdb bound state: Unbound
  compound: (R)-propane-1,2-diol
  pdb: 2bi4B01
pdb bound state: Unbound
  compound: (R)-propane-1,2-diol
  pdb: 2bl4A01
pdb bound state: Unbound
  compound: (R)-propane-1,2-diol
  pdb: 2bl4B01
pdb bound state: Analogue
  compound: (R)-propane-1,2-diol
  pdb: 1rrmA02
  ligand het code: PGO
pdb bound state: Analogue
  compound: (R)-propane-1,2-diol
  pdb: 1rrmB02
  ligand het code: PGO
pdb bound state: Unbound
  compound: (R)-propane-1,2-diol
  pdb: 2bi4A02
pdb bound state: Unbound
  compound: (R)-propane-1,2-diol
  pdb: 2bi4B02
pdb bound state: Unbound
  compound: (R)-propane-1,2-diol
  pdb: 2bl4A02
pdb bound state: Unbound
  compound: (R)-propane-1,2-diol
  pdb: 2bl4B02
pdb bound state: Unbound
  compound: (S)-propane-1,2-diol
  pdb: 1rrmA01
pdb bound state: Unbound
  compound: (S)-propane-1,2-diol
  pdb: 1rrmB01
pdb bound state: Unbound
  compound: (S)-propane-1,2-diol
  pdb: 2bi4A01
pdb bound state: Unbound
  compound: (S)-propane-1,2-diol
  pdb: 2bi4B01
pdb bound state: Unbound
  compound: (S)-propane-1,2-diol
  pdb: 2bl4A01
pdb bound state: Unbound
  compound: (S)-propane-1,2-diol
  pdb: 2bl4B01
pdb bound state: Unbound
  compound: (S)-propane-1,2-diol
  pdb: 1rrmA02
pdb bound state: Unbound
  compound: (S)-propane-1,2-diol
  pdb: 1rrmB02
pdb bound state: Unbound
  compound: (S)-propane-1,2-diol
  pdb: 2bi4A02
pdb bound state: Unbound
  compound: (S)-propane-1,2-diol
  pdb: 2bi4B02
pdb bound state: Unbound
  compound: (S)-propane-1,2-diol
  pdb: 2bl4A02
pdb bound state: Unbound
  compound: (S)-propane-1,2-diol
  pdb: 2bl4B02
pdb bound state: Analogue
  compound: NAD+
  pdb: 1rrmA01
  ligand het code: APR
pdb bound state: Analogue
  compound: NAD+
  pdb: 1rrmB01
  ligand het code: APR
pdb bound state: Unbound
  compound: NAD+
  pdb: 1rrmA02
pdb bound state: Unbound
  compound: NAD+
  pdb: 1rrmB02
pdb bound state: Unbound
  compound: NAD+
  pdb: 2bi4A02
pdb bound state: Unbound
  compound: NAD+
  pdb: 2bi4B02
pdb bound state: Unbound
  compound: NAD+
  pdb: 2bl4A02
pdb bound state: Unbound
  compound: NAD+
  pdb: 2bl4B02
pdb bound state: Unbound
  compound: Iron
  pdb: 1rrmA01
pdb bound state: Unbound
  compound: Iron
  pdb: 1rrmB01
pdb bound state: Unbound
  compound: Iron
  pdb: 2bi4A01
pdb bound state: Unbound
  compound: Iron
  pdb: 2bi4B01
pdb bound state: Unbound
  compound: Iron
  pdb: 2bl4A01
pdb bound state: Unbound
  compound: Iron
  pdb: 2bl4B01
pdb bound state: Analogue
  compound: Iron
  pdb: 1rrmA02
  ligand het code: _ZN
pdb bound state: Analogue
  compound: Iron
  pdb: 1rrmB02
  ligand het code: _ZN
pdb bound state: Unbound
  compound: Iron
  pdb: 2bl4A02
pdb bound state: Unbound
  compound: Iron
  pdb: 2bl4B02
pdb bound state: Unbound
  compound: (R)-lactaldehyde
  pdb: 1rrmA01
active site residues resources: Glycerol dehydrogenase. structure, specificity, and mechanism of a family III polyol dehydrogenase.
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00840#5
references: Molecular characterization of microbial alcohol dehydrogenases.
references: Site-directed mutagenesis studies of the metal-binding center of the iron-dependent propanediol oxidoreductase from Escherichia coli.
references: Glycerol dehydrogenase. structure, specificity, and mechanism of a family III polyol dehydrogenase.
references: Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli.
comment: This enzyme belongs to the group III "iron-activated" dehydrogenases. This enzyme is homologous to glycerol dehydrogenase (D00835 in EzCatDB), whose metal cofactor is zinc ion, instead of iron (see [3]). However, this enzyme adopts iron ion as a cofactor, with slightly different binding site from that of the homologous enyzme (see [4]). According to the literature [4], although His267 does not interact with the hydroxyl group of the substrate, it might interact with it through a water molecule. Possibly, it may act as a general base-acid. Moreover, the substrate hydroxyl group is bound to the iron ion, along with Asp196, His200, His263 and His277. The iron cofactor seems to lower the pKa of the hydroxyl group, facilitating the hydride transfer from the substrate to the nicotinamide C4 atom of NAD (see [4]).

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.1970

Dehydroquinate synthase-like, alpha domain
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.20.1090.10
catalytic domain: index.html

Pyruvate metabolism
type: KeggPathway
references: KEGG:MAP00620

Glyoxylate and dicarboxylate metabolism
type: KeggPathway
references: KEGG:MAP00630

Iron
type: KeggCofactor
references: KEGG:C00023
ec: https://purl.uniprot.org/enzyme/1.1.1.77
compound type: heavy metal
references: CHEBI:18248
references: CHEBI:82664
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

(R)-propane-1,2-diol
type: KeggSubstrate
references: KEGG:C02912
compound type: carbohydrate
references: CHEBI:28972
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

(S)-propane-1,2-diol
type: KeggSubstrate
references: KEGG:C02917
compound type: carbohydrate
references: CHEBI:29002
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NAD+
type: KeggSubstrate
references: KEGG:C00003
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:15846
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

(R)-lactaldehyde
type: KeggProduct
references: KEGG:C00937
compound type: carbohydrate
references: CHEBI:17167
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

(S)-lactaldehyde
type: KeggProduct
references: KEGG:C00424
compound type: carbohydrate
references: CHEBI:18041
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADH
type: KeggProduct
references: KEGG:C00004
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16908
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

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

1rrmA02
type: Pdb
references: 1rrm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rrm
catalytic residue: HIS 267
cofactor binding residue: ASP 196;HIS 200;HIS 263;HIS 277

1rrmB02
type: Pdb
references: 1rrm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rrm
catalytic residue: HIS 267
cofactor binding residue: ASP 196;HIS 200;HIS 263;HIS 277

2bi4A02
type: Pdb
references: 2bi4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bi4
catalytic residue: HIS 267
cofactor binding residue: ASP 196;HIS 200;HIS 263;HIS 277

2bi4B02
type: Pdb
references: 2bi4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bi4
catalytic residue: HIS 1267
cofactor binding residue: ASP 1196;HIS 1200;HIS 1263;HIS 1277

2bl4A02
type: Pdb
references: 2bl4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bl4
catalytic residue: HIS 267
cofactor binding residue: ASP 196;HIS 200;HIS 263;HIS 277

2bl4B02
type: Pdb
references: 2bl4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2bl4
catalytic residue: HIS 1267
cofactor binding residue: ASP 1196;HIS 1200;HIS 1263;HIS 1277

Molecular characterization of microbial alcohol dehydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8185833
journal: Crit Rev Microbiol
volume: 20
pages: 13-56
published year: 1994
authors:
  item: Reid MF
  item: Fewson CA

Site-directed mutagenesis studies of the metal-binding center of the iron-dependent propanediol oxidoreductase from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9851711
journal: Eur J Biochem
volume: 258
pages: 207-13
published year: 1998
authors:
  item: Obradors N
  item: Cabiscol E
  item: Aguilar J
  item: Ros J

Glycerol dehydrogenase. structure, specificity, and mechanism of a family III polyol dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11566129
journal: Structure
volume: 9
pages: 789-802
published year: 2001
authors:
  item: Ruzheinikov SN
  item: Burke J
  item: Sedelnikova S
  item: Baker PJ
  item: Taylor R
  item: Bullough PA
  item: Muir NM
  item: Gore MG
  item: Rice DW

Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15995211
journal: J Bacteriol
volume: 187
pages: 4957-66
published year: 2005
authors:
  item: Montella C
  item: Bellsolell L
  item: Perez-Luque R
  item: Badia J
  item: Baldoma L
  item: Coll M
  item: Aguilar J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

ReferenceForCatalyticMechanism
reference index: 2
reference section: p.211-212

ReferenceForCatalyticMechanism
reference index: 5
reference section: p.4960-4961