EzCatDB: D00840
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DB codeD00840
CATH domainDomain 13.40.50.1970 : Rossmann fold
Domain 21.20.1090.10 : Dehydroquinate synthase-like, alpha domainCatalytic domain
E.C.1.1.1.77

CATH domainRelated DB codes (homologues)
1.20.1090.10 : Dehydroquinate synthase-like, alpha domainD00835
3.40.50.1970 : Rossmann foldD00835

Enzyme Name
UniProtKBKEGG

P0A9S1
Protein nameLactaldehyde reductaseLactaldehyde reductase
Propanediol:nicotinamide adenine dinucleotide (NAD+) oxidoreductase
L-Lactaldehyde:propanediol oxidoreductase
SynonymsEC 1.1.1.77
Propanediol oxidoreductase
RefSeqNP_417279.2 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491007.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF00465 (Fe-ADH)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00620Pyruvate metabolism
MAP00630Glyoxylate and dicarboxylate metabolism

UniProtKB:Accession NumberP0A9S1
Entry nameFUCO_ECOLI
Activity(R)[or (S)]-propane-1,2-diol + NAD(+) = (R)[or (S)]-lactaldehyde + NADH.
Subunit
Subcellular location
CofactorIron (Potential).

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00023C02912C02917C00003C00937C00424C00004C00080
E.C.1.1.1.77






CompoundIron(R)-propane-1,2-diol(S)-propane-1,2-diolNAD+(R)-lactaldehyde(S)-lactaldehydeNADHH+
Typeheavy metalcarbohydratecarbohydrateamide group,amine group,nucleotidecarbohydratecarbohydrateamide group,amine group,nucleotideothers
ChEBI18248
82664
28972
29002
15846
17167
18041
16908
15378
PubChem23925
259994
439846
5893
439350
439231
439153
1038
                
1rrmA01UnboundUnboundUnboundAnalogue:APRUnboundUnboundUnbound 
1rrmB01UnboundUnboundUnboundAnalogue:APRUnboundUnboundUnbound 
2bi4A01UnboundUnboundUnboundBound:NADUnboundUnboundUnbound 
2bi4B01UnboundUnboundUnboundBound:NADUnboundUnboundUnbound 
2bl4A01UnboundUnboundUnboundBound:NADUnboundUnboundUnbound 
2bl4B01UnboundUnboundUnboundBound:NADUnboundUnboundUnbound 
1rrmA02Analogue:_ZNAnalogue:PGOUnboundUnboundUnboundUnboundUnbound 
1rrmB02Analogue:_ZNAnalogue:PGOUnboundUnboundUnboundUnboundUnbound 
2bi4A02Bound:_FEUnboundUnboundUnboundUnboundUnboundUnbound 
2bi4B02Bound:_FEUnboundUnboundUnboundUnboundUnboundUnbound 
2bl4A02UnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2bl4B02UnboundUnboundUnboundUnboundUnboundUnboundUnbound 

Active-site residues
resource
literature [2], [4]
pdbCatalytic residuesCofactor-binding residues
          
1rrmA01 
 
1rrmB01 
 
2bi4A01 
 
2bi4B01 
 
2bl4A01 
 
2bl4B01 
 
1rrmA02HIS  267
ASP  196;HIS  200;HIS  263;HIS  277
1rrmB02HIS  267
ASP  196;HIS  200;HIS  263;HIS  277
2bi4A02HIS  267
ASP  196;HIS  200;HIS  263;HIS  277
2bi4B02HIS 1267
ASP 1196;HIS 1200;HIS 1263;HIS 1277
2bl4A02HIS  267
ASP  196;HIS  200;HIS  263;HIS  277
2bl4B02HIS 1267
ASP 1196;HIS 1200;HIS 1263;HIS 1277

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.211-212
[5]p.4960-4961

references
[1]
PubMed ID8185833
JournalCrit Rev Microbiol
Year1994
Volume20
Pages13-56
AuthorsReid MF, Fewson CA
TitleMolecular characterization of microbial alcohol dehydrogenases.
[2]
PubMed ID9851711
JournalEur J Biochem
Year1998
Volume258
Pages207-13
AuthorsObradors N, Cabiscol E, Aguilar J, Ros J
TitleSite-directed mutagenesis studies of the metal-binding center of the iron-dependent propanediol oxidoreductase from Escherichia coli.
[3]
PubMed ID11566129
JournalStructure
Year2001
Volume9
Pages789-802
AuthorsRuzheinikov SN, Burke J, Sedelnikova S, Baker PJ, Taylor R, Bullough PA, Muir NM, Gore MG, Rice DW
TitleGlycerol dehydrogenase. structure, specificity, and mechanism of a family III polyol dehydrogenase.
[4]
PubMed ID15995211
JournalJ Bacteriol
Year2005
Volume187
Pages4957-66
AuthorsMontella C, Bellsolell L, Perez-Luque R, Badia J, Baldoma L, Coll M, Aguilar J
TitleCrystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli.
Related PDB2bi4,2bl4

comments
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]).

createdupdated
2010-02-172011-05-19


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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