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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: aldehyde reductase

Gene: SDR2 Accession Number: AT2G24190 (MetaCyc)

Synonyms: CytADR

Species: Arabidopsis thaliana col

Summary:
CytADR is an aldehyde reductase (ADR) that catalyzes the reduction of the carbonyl groups on saturated and alpha,beta-unsaturated aldehydes with 5 or more carbons in vitro. It is a member of the short-chain dehydrogenase/reductase (SDR) family of proteins [Yamauchi11].

It is believed that this enzyme localizes to the cytosol like the closely-related ADR protein where they likely help to detoxify reactive carbonyls [Yamauchi11].

Interestingly, in vitro this protein is also able to reduce methylglyoxal, an α-dicarbonyl compound that may be produced during glycolysis, fatty acid metabolism, and protein metabolism [Yamauchi11].

Two chloroplastic (ChlADR and ChlADR) as well as a second cytosolic ADR in Arabidopsis thaliana col with similar enzymatic activity have also been characterized [Yamauchi11].

Map Position: [10,290,714 -> 10,292,060]

Unification Links: PhylomeDB:Q9ZUH5 , Phytozome Plant Orthologs:AT2G24190.2 , Pride:Q9ZUH5 , Protein Model Portal:Q9ZUH5 , SMR:Q9ZUH5 , TAIR:AT2G24190 , UniProt:Q9ZUH5

Relationship Links: InterPro:IN-FAMILY:IPR002198 , InterPro:IN-FAMILY:IPR002347 , InterPro:IN-FAMILY:IPR016040 , Pfam:IN-FAMILY:PF00106 , Prints:IN-FAMILY:PR00080 , Prints:IN-FAMILY:PR00081 , Prosite:IN-FAMILY:PS00061

Gene-Reaction Schematic: ?

Gene Class: UNCLASSIFIED

Credits:
Created 01-Apr-2011 by Dreher KA , TAIR


Enzymatic reaction of: butanal reductase (aldehyde reductase)

Synonyms: butyraldehyde reductase

EC Number: 1.1.1.-

n-butanol + NADP+ <=> butanal + NADPH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible.

Summary:
The kcat for ADR for this reaction is 9.1 s-1 and the kcat/Km is 0.23 s-1 mM-1 [Yamauchi11].

Kinetic Parameters:

Substrate
Km (μM)
Citations
butanal
40000.0
[Yamauchi11]


Enzymatic reaction of: trans-2-hexenal reductase (aldehyde reductase)

EC Number: 1.1.1.-

trans-2-hexenol + NADP+ <=> trans-2-hexenal + NADPH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the opposite direction.

In Pathways: superpathway of lipoxygenase , traumatin and (Z)-3-hexen-1-yl acetate biosynthesis

Summary:
The kcat for ADR for this reaction is 0.6 s-1 and the kcat/Km is 0.35 s-1 mM-1 [Yamauchi11].

Kinetic Parameters:

Substrate
Km (μM)
Citations
trans-2-hexenal
1700.0
[Yamauchi11]


Enzymatic reaction of: trans-2-pentenal reductase (aldehyde reductase)

EC Number: 1.1.1.-

trans-2-pentenol + NADP+ <=> trans-2-pentenal + NADPH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the opposite direction.

Summary:
The kcat for ADR for this reaction is 0.4 s-1 and the kcat/Km is 2.0 s-1 mM-1 [Yamauchi11].

Kinetic Parameters:

Substrate
Km (μM)
Citations
trans-2-pentenal
200.0
[Yamauchi11]


Enzymatic reaction of: methylglyoxal reductase (aldehyde reductase)

EC Number: 1.1.1.-

acetol + NADP+ <=> methylglyoxal + NADPH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible.

Summary:
The kcat for ADR for this reaction is 24 s-1 and the kcat/Km is 0.35 s-1 mM-1 [Yamauchi11].

Kinetic Parameters:

Substrate
Km (μM)
Citations
methylglyoxal
69000.0
[Yamauchi11]


References

Yamauchi11: Yamauchi Y, Hasegawa A, Taninaka A, Mizutani M, Sugimoto Y (2011). "NADPH-dependent Reductases Involved in the Detoxification of Reactive Carbonyls in Plants." J Biol Chem 286(9);6999-7009. PMID: 21169366


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, biocyc14.