ALO1/YML086C Summary Help

ALO1 BASIC INFORMATION

Standard Name ALO1
Systematic Name YML086C
Feature Type ORF, Verified
Description D-Arabinono-1,4-lactone oxidase, catalyzes the final step in biosynthesis of dehydro-D-arabinono-1,4-lactone, which is protective against oxidative stress (1 and see Summary Paragraph)
Name Description D-Arabinono-1,4-Lactone Oxidase 1
GO Annotations All ALO1 GO evidence and references
    View Computational GO annotations for ALO1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Pathways
Mutant Phenotype All ALO1 Phenotype details and references
Classical genetics
null
overexpression
Large-scale survey
null
overexpression
Interactions ALO1 All interactions details and references
42 total interaction(s) for 41 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 4
  • Affinity Capture-RNA: 1
  • Biochemical Activity: 2
  • Co-fractionation: 1
  • PCA: 34
Sequence Information
ChrXIII:97371 to 95791 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1581 97371..95791 1996-07-31 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000004551

ALO1 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Sequence Analysis Tools
  • Protein Info & Structure
  • Localization Resources
  • Interactions
  • Phenotype Resources
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  • Comparison Resources
  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for ALO1

SUMMARY PARAGRAPH for ALO1

ALO1 encodes D-arabinono-1,4-lactone oxidase (called ALO in other organisms) (EC 1.1.3.37), a mitochondrial protein (1, 2) that converts D-arabinono-1,4-lactone to dehydro-D-arabinono-1,4-lactone, the enantiomer of ascorbate (vitamin C) (3, 4). Saccharomyces cerevisiae does not normally synthesize ascorbate, but Alo1p is sufficiently promiscuous that it can convert a number of related substrates to either dehydro-D-arabinono-1,4-lactone or ascorbate, depending on the chirality of the substrate (1, 5, 6). Like ascorbate, dehydro-D-arabinono-1,4-lactone is an antioxidant. Deletion of ALO1 results in increased sensitivity to oxidative stress (1) and an increased rate of gross chromosomal rearrangements, implying that Alo1p suppresses oxidative damage of DNA (7). Transcription of ALO1 is not regulated in response to oxidative stress (1). Alo1p exists as a monomer embedded in the mitochondrial membrane (1) and binds FAD (1, 8).

Please note: There is a history of disagreement regarding the name of the product synthesized by Alo1p. It has been called D-erythroascorbic acid (or D-erythroascorbate) in the literature (1, 9). The ChEBI chemical database at the European Bioinformatics Institute (see http://www.ebi.ac.uk/chebi/searchFreeText.do?searchString=17803 ) changed the name to dehydro-D-arabinono-1,4-lactone in 2008, based on the advice of the International Union of Biochemistry and Molecular Biology (IUBMB; see http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/1/3/37.html ). The IUBMB changed the name from D-erythroascorbate to dehydro-D-arabinono-1,4-lactone in May 2008, because they decided that the name D-erythroascorbate refers to a 6-carbon compound and not a 5-carbon compound as the product is described in the literature (1).

Last updated: 2009-02-02

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for ALO1]

1) Huh WK, et al.  (1998) D-Erythroascorbic acid is an important antioxidant molecule in Saccharomyces cerevisiae. Mol Microbiol 30(4):895-903
2) Sickmann A, et al.  (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc Natl Acad Sci U S A 100(23):13207-12
3) Nishikimi M, et al.  (1978) Occurrence in yeast of L-galactonolactone oxidase which is similar to a key enzyme for ascorbic acid biosynthesis in animals, L-gulonolactone oxidase. Arch Biochem Biophys 191(2):479-86
4) Kenney WC, et al.  (1979) Identification of the covalently-bound flavin of L-galactonolactone oxidase from yeast. FEBS Lett 97(1):40-2
5) Sauer M, et al.  (2004) Production of L-ascorbic acid by metabolically engineered Saccharomyces cerevisiae and Zygosaccharomyces bailii. Appl Environ Microbiol 70(10):6086-91
6) Hancock RD, et al.  (2000) Biosynthesis of L-ascorbic acid (vitamin C) by Saccharomyces cerevisiae. FEMS Microbiol Lett 186(2):245-50
7) Smith S, et al.  (2004) Mutator genes for suppression of gross chromosomal rearrangements identified by a genome-wide screening in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 101(24):9039-44
8) Lee BH, et al.  (1999) Bacterial production of D-erythroascorbic acid and L-ascorbic acid through functional expression of Saccharomyces cerevisiae D-arabinono-1,4-lactone oxidase in Escherichia coli. Appl Environ Microbiol 65(10):4685-7
9) Amako K, et al.  (2006) NAD(+)-specific d-arabinose dehydrogenase and its contribution to erythroascorbic acid production in Saccharomyces cerevisiae. FEBS Lett 580(27):6428-34