Glycerol dehydrogenase

 

Glycerol dehydrogenase catalyses the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). This reaction allows microorganisms to utilise glycerol as a source of carbon under anaerobic conditions.

 

Reference Protein and Structure

Sequence
Q9WYQ4 UniProt (1.1.1.6) IPR001670 (Sequence Homologues) (PDB Homologues)
Biological species
Thermotoga maritima MSB8 (Bacteria) Uniprot
PDB
1kq3 - CRYSTAL STRUCTURE OF A GLYCEROL DEHYDROGENASE (TM0423) FROM THERMOTOGA MARITIMA AT 1.5 A RESOLUTION (1.5 Å) PDBe PDBsum 1kq3
Catalytic CATH Domains
1.20.1090.10 CATHdb (see all for 1kq3)
Cofactors
Zinc(2+) (1) Metal MACiE
Click To Show Structure

Enzyme Reaction (EC:1.1.1.6)

NAD(1-)
CHEBI:57540ChEBI
+
glycerol
CHEBI:17754ChEBI
hydron
CHEBI:15378ChEBI
+
NADH(2-)
CHEBI:57945ChEBI
+
dihydroxyacetone
CHEBI:16016ChEBI
Alternative enzyme names: NAD-linked glycerol dehydrogenase, Glycerin dehydrogenase,

Enzyme Mechanism

Introduction

A bound water molecule (activated by His255) abstracts a proton from the zinc-boud hydroxyl group of the substrate. This eliminates a hydride ion that is transferred to NAD.

Catalytic Residues Roles

UniProt PDB* (1kq3)
His255 His255(267)A Increases the basicity of a water molecule. Although it has been suggested that the water molecule may be part of a proton relay chain, there is no direct evidence (other than the crystal structure) that His255 actually acts as a general acid/base. increase basicity, hydrogen bond acceptor
Asp169, His252, His269 Asp169(181)A, His252(264)A, His269(281)A Forms part of the catalytic zinc binding site. metal ligand
*PDB label guide - RESx(y)B(C) - RES: Residue Name; x: Residue ID in PDB file; y: Residue ID in PDB sequence if different from PDB file; B: PDB Chain; C: Biological Assembly Chain if different from PDB. If label is "Not Found" it means this residue is not found in the reference PDB.

Chemical Components

proton transfer, hydride transfer, bimolecular elimination, bimolecular nucleophilic addition, overall reactant used, overall product formed

References

  1. Ruzheinikov SN et al. (2001), Structure, 9, 789-802. Glycerol dehydrogenase. structure, specificity, and mechanism of a family III polyol dehydrogenase. PMID:11566129.

Catalytic Residues Roles

Residue Roles
His255(267)A hydrogen bond acceptor, increase basicity
Asp169(181)A metal ligand
His252(264)A metal ligand
His269(281)A metal ligand

Chemical Components

proton transfer, hydride transfer, ingold: bimolecular elimination, ingold: bimolecular nucleophilic addition, overall reactant used, overall product formed

Contributors

Gemma L. Holliday