Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.26 extracted from

  • Hoover, G.J.; Jorgensen, R.; Rochon, A.; Bajwa, V.S.; Merrill, A.R.; Shelp, B.J.
    Identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants (2013), Biochim. Biophys. Acta, 1834, 2663-2671.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome
-
Arabidopsis thaliana 5777
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycolate + NAD+ Arabidopsis thaliana
-
glyoxylate + NADH + H+
-
r
additional information Arabidopsis thaliana the recombinant AtHPR1 prefers prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate ?
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9C9W5 cf. EC 1.1.1.29
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycolate + NAD+
-
Arabidopsis thaliana glyoxylate + NADH + H+
-
r
additional information the recombinant AtHPR1 prefers prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate Arabidopsis thaliana ?
-
?

Synonyms

Synonyms Comment Organism
glycerate dehydrogenase
-
Arabidopsis thaliana
HPR1
-
Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Arabidopsis thaliana
NADH
-
Arabidopsis thaliana

General Information

General Information Comment Organism
evolution the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs Arabidopsis thaliana