MetaCyc Enzyme: NAD(P)+ L-lactaldehyde dehydrogenase

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

Synonyms: PICST_29563, ALD5

Species: Scheffersomyces stipitis CBS 6054

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 [Watanabe08].

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 [Watanabe08].

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 [Watanabe08].

Molecular Weight of Polypeptide: 53.49 kD (from nucleotide sequence), 55.0 kD (experimental) [Watanabe08 ]

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 , InterPro:IN-FAMILY:IPR029510 , Pfam:IN-FAMILY:PF00171 , Prosite:IN-FAMILY:PS00070 , Prosite:IN-FAMILY:PS00687

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Created 16-Feb-2011 by Fulcher CA , SRI International

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

EC Number:

(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 [Watanabe08 ] , pentanal [Watanabe08 ] , acetaldehyde [Watanabe08 ] , propanal [Watanabe08 ] , (R)-lactaldehyde [Watanabe08 ] , formaldehyde [Watanabe08 ] , hexanal [Watanabe08 ] , heptanal [Watanabe08 ] , octanal [Watanabe08 ] , isobutanal [Watanabe08 ] , D-glyceraldehyde [Watanabe08 ] , D-glyceraldehyde 3-phosphate [Watanabe08 ] , benzaldehyde [Watanabe08 ] , betaine aldehyde [Watanabe08 ] , glutaraldehyde [Watanabe08 ] , glycolaldehyde [Watanabe08 ]

In Pathways: L-rhamnose degradation II

Unlike EC, 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 [Watanabe08].

Kinetic Parameters:

Km (μM)

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


Watanabe08: 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 19.0 on Fri May 29, 2015, BIOCYC13B.