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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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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 Fri Dec 19, 2014, BIOCYC14A.