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Glyoxylate reductase

Glyoxylate Reductase
Crystal Structure of Glyoxylate Reductase.png
The crystal structure of glyoxylate reductase complexed with NADPH. Each color represents a monomer of the enzyme. This enzyme was isolated from a hyperthermophilic archaeon, Pyrococcus horikoshii OT3. Image created by PyMOL.
Identifiers
EC number 1.1.1.26
CAS number 9028-32-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

Glyoxylate reductase (EC 1.1.1.26), first isolated from spinach leaves, is an enzyme that catalyzes the reduction of glyoxylate to glycolate, using the cofactor NADH or NADPH.

The systematic name of this enzyme class is glycolate:NAD+ oxidoreductase. Other names in common use include NADH-glyoxylate reductase, glyoxylic acid reductase, and NADH-dependent glyoxylate reductase.

The crystal structure of the glyoxylate reductase enzyme from the hyperthermophilic archeon Pyrococcus horiskoshii OT3 has been reported. The enzyme exists in the dimeric form. Each monomer has two domains: a substrate-binding domain where glyoxylate binds, and a nucleotide-binding domain where the NAD(P)H cofactor binds.

The enzyme catalyzes the transfer of a hydride from NAD(P)H to glyoxylate, causing a reduction of the substrate to glycolate and an oxidation of the cofactor to NAD(P)+. Figure 2 shows the mechanism for this reaction.

It is thought that the two residues Glu270 and His288 are important for the enzyme's catalytic function, while the residue Arg241 is thought to be important for substrate specificity.

The glyoxylate reductase enzyme localizes to the cell cytoplasm in plants. It can use both NADPH and NADH as a cofactor, but prefers NADPH. The enzyme substrate, glyoxylate, is a metabolite in plant photorespiration, and is produced in the peroxisome. Glyoxylate is important in the plant cell as it can deactivate RUBISCO and inhibit its activation. Hence, glyoxylate levels are important in regulating photosynthesis.


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Wikipedia

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