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Literature summary for 2.5.1.47 extracted from

  • Salbitani, G.; Wirtz, M.; Hell, R.; Carfagna, S.
    Affinity purification of O-acetylserine(thiol)lyase from Chlorella sorokiniana by recombinant proteins from Arabidopsis thaliana (2014), Metabolites, 4, 629-639.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of chloroplast isozyme OASTL in Arabidopsis thaliana transgenic plants. The cytosolic AtSAT5 isoform from Arabidopsis thaliana is N-terminaly fused with a His-tag, expressed in Escherichia coli and immobilized on a His-trap column for use as affinity anchor to purify enzyme OASTL Chlorella sorokiniana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Chlorella sorokiniana 9507
-
cytosol
-
Chlorella sorokiniana 5829
-
additional information in the unicellular green alga Chlorella sorokiniana two OASTL isoforms, chloroplastic and cytosolic, occur among which the cytosolic is induced under S-deprivation, uniquely altered amounts and activities of OASTL during S-starvation as opposed to the vascular plant systems, e.g. a 17fold increase in the specific activity of enzyme OASTL Chlorella sorokiniana
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31900
-
-
Chlorella sorokiniana
33800
-
-
Chlorella sorokiniana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
O-acetyl-L-serine + hydrogen sulfide Chlorella sorokiniana
-
L-cysteine + acetate
-
?
O-acetyl-L-serine + hydrogen sulfide Chlorella sorokiniana 211/8 K
-
L-cysteine + acetate
-
?

Organism

Organism UniProt Comment Textmining
Chlorella sorokiniana
-
-
-
Chlorella sorokiniana 211/8 K
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant chloroplast isozyme OASTL 29fold from Chlorella sorokiniana S-sufficient and S-starved cells by affinity binding to Arabidopsis thaliana serine acetyltransferase SAT5 fused to a metal resin via its His-tag protein, elution by by O-acetylserine, to homogeneity. Successful application of SAT/OASTL interaction for purification Chlorella sorokiniana

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
149
-
purified recombinant enzyme, pH 7.5, temperature not specified in the publication Chlorella sorokiniana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-acetyl-L-serine + hydrogen sulfide
-
Chlorella sorokiniana L-cysteine + acetate
-
?
O-acetyl-L-serine + hydrogen sulfide
-
Chlorella sorokiniana 211/8 K L-cysteine + acetate
-
?

Subunits

Subunits Comment Organism
? x * 33800, chloroplast isozyme OASTL, SDS-PAGE, x * 31900, cytosolic isozyme OASTL, SDS-PAGE Chlorella sorokiniana

Synonyms

Synonyms Comment Organism
O-acetylserine(thiol)lyase
-
Chlorella sorokiniana
OASTL
-
Chlorella sorokiniana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Chlorella sorokiniana

Expression

Organism Comment Expression
Chlorella sorokiniana S-starvation results in the increase of the larger chloroplastic OASTL isoform and the induction of a new and smaller cytosolic isoform up

General Information

General Information Comment Organism
metabolism key enzyme in the biosynthetic cysteine pathway Chlorella sorokiniana
physiological function occurrence of the regulatory cysteine synthase complex in microalgae. In plants and also in bacteria, enzyme OASTL is catalytically inactive in the cysteine synthase complex but becomes fully active upon dissociation from the complex realized by O-acetylserine Chlorella sorokiniana