Gene_locus Report for: wiccf-k0ksn3

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Fungi: N E > Dikarya: N E > Ascomycota: N E > saccharomyceta: N E > Saccharomycotina: N E > Saccharomycetes: N E > Saccharomycetales: N E > Phaffomycetaceae: N E > Wickerhamomyces: N E > Wickerhamomyces ciferrii: N E

Title: Ethyl acetate production by the elusive alcohol acetyltransferase from yeast
Kruis AJ, Levisson M, Mars AE, Van der Ploeg M, Garces Daza F, Ellena V, Kengen SWM, Van der Oost J, Weusthuis RA
Ref: Metab Eng, 41:92, 2017 : PubMed
Abstract


ESTHER: Kruis_2017_Metab.Eng_41_92
PubMedSearch: Kruis 2017 Metab.Eng 41 92
PubMedID: 28356220
Gene_locus related to this paper: wicao-a0a1e3p8s6, wiccf-k0kpv8, wicao-a0a1e3p8s8, wiccf-k0ksn3, cybfa-a0a061ayy2

Abstract

Ethyl acetate is an industrially relevant ester that is currently produced exclusively through unsustainable processes. Many yeasts are able to produce ethyl acetate, but the main responsible enzyme has remained elusive, hampering the engineering of novel production strains. Here we describe the discovery of a new enzyme (Eat1) from the yeast Wickerhamomyces anomalus that resulted in high ethyl acetate production when expressed in Saccharomyces cerevisiae and Escherichia coli. Purified Eat1 showed alcohol acetyltransferase activity with ethanol and acetyl-CoA. Homologs of eat1 are responsible for most ethyl acetate synthesis in known ethyl acetate-producing yeasts, including S. cerevisiae, and are only distantly related to known alcohol acetyltransferases. Eat1 is therefore proposed to compose a novel alcohol acetyltransferase family within the alpha/beta hydrolase superfamily. The discovery of this novel enzyme family is a crucial step towards the development of biobased ethyl acetate production and will also help in selecting improved S. cerevisiae brewing strains.



        

Title: Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10
Schneider J, Andrea H, Blom J, Jaenicke S, Ruckert C, Schorsch C, Szczepanowski R, Farwick M, Goesmann A and Brinkrolf K <4 more author(s)> Schneider J, Andrea H, Blom J, Jaenicke S, Ruckert C, Schorsch C, Szczepanowski R, Farwick M, Goesmann A, Puhler A, Schaffer S, Tauch A, Kohler T, Brinkrolf K (- 4)
Ref: Eukaryot Cell, 11:1582, 2012 : PubMed
Abstract


ESTHER: Schneider_2012_Eukaryot.Cell_11_1582
PubMedSearch: Schneider 2012 Eukaryot.Cell 11 1582
PubMedID: 23193139
Gene_locus related to this paper: wiccf-k0k780, wiccf-k0kcu3, wiccf-k0kir4, wiccf-k0kmk9, wiccf-k0kn23, wiccf-k0krq2, wiccf-k0ksx2, wiccf-k0kpv8, wiccf-k0ksn3, wiccf-k0kqu5

Abstract

Wickerhamomyces ciferrii is a microorganism characterized by the production and secretion of large amounts of acetylated sphingoid bases, in particular tetraacetyl phytosphingosine. Here, we present the 15.90-Mbp draft genome sequence of W. ciferrii NRRL Y-1031 F-60-10 generated by pyrosequencing and de novo assembly. The draft genome sequence comprising 364 contigs in 150 scaffolds was annotated and covered 6,702 protein-coding sequences. This information will contribute to the metabolic engineering of this yeast to improve the yield and spectrum of acetylated sphingoid bases in biotechnological production.