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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: NAD(P)+ L-lactaldehyde dehydrogenase

Gene: LADH Accession Number: G-12538 (MetaCyc)

Synonyms: PICST_29563, ALD5

Species: Scheffersomyces stipitis CBS 6054

Summary:
The subunit structure of this enzyme has not been reported.

In Scheffersomyces stipitis CBS 6054 (previously known as Pichia stipitis CBS 6054) (S)-lactaldehyde is a product of an alternative rhamnose degradation pathway found in some bacteria and fungi (see pathway L-rhamnose degradation II). This pathway is the significant physiological origin of (S)-lactaldehyde in fungi. This enzyme was shown to catalyze the dehydrogenation of (S)-lactaldehyde to (S)-lactate (L-lactate) in cells grown on L-rhamnose, demonstrating the metabolic fate of (S)-lactaldehyde in this organism. The encoding gene was identified by mass spectrometry techniques [Watanabe08a].

Among members of the aldehyde dehydrogenase superfamily, this fungal enzyme was 34% identical to the Escherichia coli enzyme. Differences between this fungal enzyme and the Azotobacter vinelandii NBRC 102612 enzyme (see NAD+-dependent L-lactaldehyde dehydrogenase) suggested convergent evolution of fungal and bacterial L-lactaldehyde dehydrogenases [Watanabe08a].

Native enzyme was purified from Scheffersomyces stipitis CBS 6054 cells grown on L-rhamnose as sole carbon source. Recombinant, His6-tagged enzyme was overexpressed in Escherichia coli and characterized [Watanabe08a].

Molecular Weight of Polypeptide: 53.49 kD (from nucleotide sequence), 55.0 kD (experimental) [Watanabe08a ]

Unification Links: Entrez:ABN64318 , Pride:A3LNE3 , Protein Model Portal:A3LNE3 , String:4924.PICST_29563 , UniProt:A3LNE3

Relationship Links: Entrez-Nucleotide:PART-OF:CP000496 , InterPro:IN-FAMILY:IPR015590 , InterPro:IN-FAMILY:IPR016160 , 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 16-Feb-2011 by Fulcher CA , SRI International


Enzymatic reaction of: NAD+ L-lactaldehyde dehydrogenase (NAD(P)+ L-lactaldehyde dehydrogenase)

EC Number: 1.2.1.22

(S)-lactaldehyde + NAD+ + H2O <=> (S)-lactate + NADH + 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.

Alternative Substrates for (S)-lactaldehyde: butanal [Watanabe08a ] , pentanal [Watanabe08a ] , acetaldehyde [Watanabe08a ] , propanal [Watanabe08a ] , (R)-lactaldehyde [Watanabe08a ] , formaldehyde [Watanabe08a ] , hexanal [Watanabe08a ] , heptanal [Watanabe08a ] , octanal [Watanabe08a ] , isobutanal [Watanabe08a ] , D-glyceraldehyde [Watanabe08a ] , D-glyceraldehyde 3-phosphate [Watanabe08a ] , benzaldehyde [Watanabe08a ] , betaine aldehyde [Watanabe08a ] , glutaraldehyde [Watanabe08a ] , glycolaldehyde [Watanabe08a ]

In Pathways: L-rhamnose degradation II

Summary:
Unlike EC 1.2.1.22, this enzyme could utilize either NAD+ or NADP+ as cofactor, but preferred NAD+. The Kcat/Km value for NAD+ was 32.4 and for NADP+ was 20.0 (min-1 μM-1), respectively. Of various aldehydes tested, (S)-lactaldehyde was the best substrate for this enzyme although the enzyme had a relatively broad substrate specificity [Watanabe08a].

Kinetic Parameters:

Substrate
Km (μM)
Citations
(S)-lactaldehyde
42.8
[Watanabe08a]


Enzymatic reaction of: NADP+L-lactaldehyde dehydrogenase (NAD(P)+ L-lactaldehyde dehydrogenase)

EC Number: 1.2.1.-

(S)-lactaldehyde + NADP+ + H2O <=> (S)-lactate + NADPH + 2 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 direction shown.

In Pathways: L-rhamnose degradation II


References

Watanabe08a: Watanabe S, Piyanart S, Makino K (2008). "Metabolic fate of L-lactaldehyde derived from an alternative L-rhamnose pathway." FEBS J 275(20);5139-49. PMID: 18793327


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 Tue Nov 25, 2014, biocyc13.