Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: α-ketoglutarate semialdehyde dehydrogenase

Gene: ACIAD0131 Accession Number: G-11996 (MetaCyc)

Species: Acinetobacter sp. ADP1

Subunit composition of α-ketoglutarate semialdehyde dehydrogenase = [ACIAD0131]2
         α-ketoglutarate semialdehyde dehydrogenase subunit = ACIAD0131

Summary:
The enzyme from Acinetobacter sp. ADP1 (Acinetobacter baylyi ADP1) was reported to be a homodimer based on gel filtration data, but the native apparent molecular mass was not given [Aghaie08].

Recombinant enzyme was overexpressed in Escherichia coli and purified [Aghaie08].
Note that [Aghaie08] provided a subunit apparent molecular mass of 62 kDa as determined by SDS-PAGE, along with a calculated molecular mass of 58.48 kDa. A computed molecular mass of 56.145 kDa was found for this entry in the UniProt link below dated 2004.
The gene is designated here by its locus tag.

Map Position: [135,198 -> 136,778]

Molecular Weight of Polypeptide: 58.48 kD (from nucleotide sequence), 62.0 kD (experimental) [Aghaie08 ]

Unification Links: Entrez-gene:2880252 , Protein Model Portal:Q6FFQ0 , String:62977.ACIAD0131 , UniProt:Q6FFQ0

Relationship Links: InterPro:IN-FAMILY:IPR015590 , InterPro:IN-FAMILY:IPR016161 , InterPro:IN-FAMILY:IPR016162 , InterPro:IN-FAMILY:IPR016163 , Pfam:IN-FAMILY:PF00171 , Prosite:IN-FAMILY:PS00070 , Prosite:IN-FAMILY:PS00687

Gene-Reaction Schematic: ?

Credits:
Created 26-Apr-2010 by Fulcher CA , SRI International
Revised 27-Apr-2010 by Fulcher CA , SRI International


Enzymatic reaction of: α-ketoglutarate semialdehyde dehydrogenase

Synonyms: 2-ketoglutarate semialdehyde dehydrogenase

EC Number: 1.2.1.26

2,5-dioxopentanoate + NADP+ + H2O <=> 2-oxoglutarate + NADPH + 2 H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of microbial D-galacturonate and D-glucuronate degradation , D-galactarate degradation II , D-glucarate degradation II

Summary:
Depending upon the assay, the kinetics of the reaction were either sigmoidal, or hyperbolic. In contrast, a Pseudomonas putida α-ketoglutarate semialdehyde dehydrogenase isozyme encoded by locus tag PP3602 showed only hyperbolic kinetics. Although the enzyme was active with both NAD+ and NADP+, it was 58 times more active with NADP+. The Km value shown here was determined from a hyperbolic Vmax model with NADP+. The enzyme was relatively substrate-specific [Aghaie08].

Kinetic Parameters:

Substrate
Km (μM)
Citations
2,5-dioxopentanoate
15.0
[Aghaie08]


References

Aghaie08: Aghaie A, Lechaplais C, Sirven P, Tricot S, Besnard-Gonnet M, Muselet D, de Berardinis V, Kreimeyer A, Gyapay G, Salanoubat M, Perret A (2008). "New insights into the alternative D-glucarate degradation pathway." J Biol Chem 283(23);15638-46. PMID: 18364348


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, biocyc13.