Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

EC Number Cloned (Comment) Organism
2.5.1.47 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

EC Number Localization Comment Organism GeneOntology No. Textmining
2.5.1.47 chloroplast
-
 Chlorella sorokiniana 9507
-
2.5.1.47 cytosol
-
 Chlorella sorokiniana 5829
-
2.5.1.47 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.47 31900
-
-
 Chlorella sorokiniana
2.5.1.47 33800
-
-
 Chlorella sorokiniana

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.47 Chlorella sorokiniana
-
-
-
2.5.1.47 Chlorella sorokiniana 211/8 K
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.47 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5.1.47 149
-
 purified recombinant enzyme, pH 7.5, temperature not specified in the publication Chlorella sorokiniana

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.47 7.5
-
 assay at Chlorella sorokiniana

Expression

EC Number Organism Comment Expression
2.5.1.47 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

EC Number General Information Comment Organism
2.5.1.47 metabolism key enzyme in the biosynthetic cysteine pathway Chlorella sorokiniana
2.5.1.47 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