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Literature summary extracted from

  • Campanini, B.; Benoni, R.; Bettati, S.; Beck, C.M.; Hayes, C.S.; Mozzarelli, A.
    Moonlighting O-acetylserine sulfhydrylase: new functions for an old protein (2015), Biochim. Biophys. Acta, 1854, 1184-1193.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site Staphylococcus aureus
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site Haemophilus influenzae
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site Arabidopsis thaliana
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site Mycobacterium tuberculosis
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site Bacillus subtilis
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site Escherichia coli
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site Caenorhabditis elegans
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site Entamoeba histolytica
2.5.1.47 serine acetyltransferase CysE, each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. 20fold increase in catalytic efficiency upon binding of CysE to CysK as a result of both decreased KM for acetyl-CoA and increased kcat. Free CysE enzyme is less active and more susceptible to aggregation, inactivation and proteolysis Glycine max

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.47 additional information CysK is competitively inhibited within the cysteine synthase complex Glycine max

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 Staphylococcus aureus
-
 L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide Salmonella enterica subsp. enterica serovar Typhimurium
-
 L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide Glycine max
-
 L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide Haemophilus influenzae
-
 L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide Arabidopsis thaliana
-
 L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide Mycobacterium tuberculosis
-
 L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide Bacillus subtilis
-
 L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide Escherichia coli
-
 L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide Caenorhabditis elegans
-
 L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide Entamoeba histolytica
-
 L-cysteine + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.47 Arabidopsis thaliana P47998 gene cysK
-
2.5.1.47 Bacillus subtilis P37887 gene cysK
-
2.5.1.47 Caenorhabditis elegans Q93244 gene cysK
-
2.5.1.47 Entamoeba histolytica Q401L7
-
-
2.5.1.47 Escherichia coli P0ABK5 gene cysK
-
2.5.1.47 Glycine max A3RM03 gene cysK
-
2.5.1.47 Haemophilus influenzae P45040
-
-
2.5.1.47 Mycobacterium tuberculosis P9WP55
-
-
2.5.1.47 Salmonella enterica subsp. enterica serovar Typhimurium P0A1E3 gene cysK
-
2.5.1.47 Staphylococcus aureus
-
-
-

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
-
 Staphylococcus aureus L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide
-
 Salmonella enterica subsp. enterica serovar Typhimurium L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide
-
 Glycine max L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide
-
 Haemophilus influenzae L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide
-
 Arabidopsis thaliana L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide
-
 Mycobacterium tuberculosis L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide
-
 Bacillus subtilis L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide
-
 Escherichia coli L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide
-
 Caenorhabditis elegans L-cysteine + acetate
-
 ?
2.5.1.47 O-acetyl-L-serine + hydrogen sulfide
-
 Entamoeba histolytica L-cysteine + acetate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.47 cysK
-
 Staphylococcus aureus
2.5.1.47 cysK
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 cysK
-
 Glycine max
2.5.1.47 cysK
-
 Haemophilus influenzae
2.5.1.47 cysK
-
 Arabidopsis thaliana
2.5.1.47 cysK
-
 Mycobacterium tuberculosis
2.5.1.47 cysK
-
 Bacillus subtilis
2.5.1.47 cysK
-
 Escherichia coli
2.5.1.47 cysK
-
 Caenorhabditis elegans
2.5.1.47 cysK
-
 Entamoeba histolytica
2.5.1.47 O-acetylserine sulfhydrylase
-
 Staphylococcus aureus
2.5.1.47 O-acetylserine sulfhydrylase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 O-acetylserine sulfhydrylase
-
 Glycine max
2.5.1.47 O-acetylserine sulfhydrylase
-
 Haemophilus influenzae
2.5.1.47 O-acetylserine sulfhydrylase
-
 Arabidopsis thaliana
2.5.1.47 O-acetylserine sulfhydrylase
-
 Mycobacterium tuberculosis
2.5.1.47 O-acetylserine sulfhydrylase
-
 Bacillus subtilis
2.5.1.47 O-acetylserine sulfhydrylase
-
 Escherichia coli
2.5.1.47 O-acetylserine sulfhydrylase
-
 Caenorhabditis elegans
2.5.1.47 O-acetylserine sulfhydrylase
-
 Entamoeba histolytica
2.5.1.47 O-acetylserine sulfhydrylase A
-
 Staphylococcus aureus
2.5.1.47 O-acetylserine sulfhydrylase A
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 O-acetylserine sulfhydrylase A
-
 Glycine max
2.5.1.47 O-acetylserine sulfhydrylase A
-
 Haemophilus influenzae
2.5.1.47 O-acetylserine sulfhydrylase A
-
 Arabidopsis thaliana
2.5.1.47 O-acetylserine sulfhydrylase A
-
 Mycobacterium tuberculosis
2.5.1.47 O-acetylserine sulfhydrylase A
-
 Bacillus subtilis
2.5.1.47 O-acetylserine sulfhydrylase A
-
 Escherichia coli
2.5.1.47 O-acetylserine sulfhydrylase A
-
 Caenorhabditis elegans
2.5.1.47 O-acetylserine sulfhydrylase A
-
 Entamoeba histolytica
2.5.1.47 OASS
-
 Staphylococcus aureus
2.5.1.47 OASS
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 OASS
-
 Glycine max
2.5.1.47 OASS
-
 Haemophilus influenzae
2.5.1.47 OASS
-
 Arabidopsis thaliana
2.5.1.47 OASS
-
 Mycobacterium tuberculosis
2.5.1.47 OASS
-
 Bacillus subtilis
2.5.1.47 OASS
-
 Escherichia coli
2.5.1.47 OASS
-
 Caenorhabditis elegans
2.5.1.47 OASS
-
 Entamoeba histolytica

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.47 pyridoxal 5'-phosphate dependent on Staphylococcus aureus
2.5.1.47 pyridoxal 5'-phosphate dependent on Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 pyridoxal 5'-phosphate dependent on Glycine max
2.5.1.47 pyridoxal 5'-phosphate dependent on Haemophilus influenzae
2.5.1.47 pyridoxal 5'-phosphate dependent on Arabidopsis thaliana
2.5.1.47 pyridoxal 5'-phosphate dependent on Mycobacterium tuberculosis
2.5.1.47 pyridoxal 5'-phosphate dependent on Bacillus subtilis
2.5.1.47 pyridoxal 5'-phosphate dependent on Escherichia coli
2.5.1.47 pyridoxal 5'-phosphate dependent on Caenorhabditis elegans
2.5.1.47 pyridoxal 5'-phosphate dependent on Entamoeba histolytica

General Information

EC Number General Information Comment Organism
2.5.1.47 evolution the CysK/CysE binding interaction is conserved in most bacterial and plant systems Staphylococcus aureus
2.5.1.47 evolution the CysK/CysE binding interaction is conserved in most bacterial and plant systems Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 evolution the CysK/CysE binding interaction is conserved in most bacterial and plant systems Glycine max
2.5.1.47 evolution the CysK/CysE binding interaction is conserved in most bacterial and plant systems Haemophilus influenzae
2.5.1.47 evolution the CysK/CysE binding interaction is conserved in most bacterial and plant systems Arabidopsis thaliana
2.5.1.47 evolution the CysK/CysE binding interaction is conserved in most bacterial and plant systems Mycobacterium tuberculosis
2.5.1.47 evolution the CysK/CysE binding interaction is conserved in most bacterial and plant systems Bacillus subtilis
2.5.1.47 evolution the CysK/CysE binding interaction is conserved in most bacterial and plant systems Escherichia coli
2.5.1.47 evolution the CysK/CysE binding interaction is conserved in most bacterial and plant systems Caenorhabditis elegans
2.5.1.47 evolution the CysK/CysE binding interaction is conserved in most bacterial and plant systems Entamoeba histolytica
2.5.1.47 malfunction deletion of the C-terminal Ile, or substitution with Ala or Glu, in CysE consistently impairs complex formation with CysK Mycobacterium tuberculosis
2.5.1.47 metabolism the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview Staphylococcus aureus
2.5.1.47 metabolism the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 metabolism the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview Glycine max
2.5.1.47 metabolism the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview Haemophilus influenzae
2.5.1.47 metabolism the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview Arabidopsis thaliana
2.5.1.47 metabolism the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview Mycobacterium tuberculosis
2.5.1.47 metabolism the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview Bacillus subtilis
2.5.1.47 metabolism the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview Escherichia coli
2.5.1.47 metabolism the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview Entamoeba histolytica
2.5.1.47 metabolism the enzyme catalyzes the final reaction of cysteine biosynthesis. Biological roles of known CysK complexes in the context of cysteine metabolism, overview Caenorhabditis elegans
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific Staphylococcus aureus
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific Bacillus subtilis
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific Escherichia coli
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific Caenorhabditis elegans
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific, interaction analysis and binding structure Glycine max
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific, interaction analysis and binding structure. Negative cooperativity with decapeptide binding to AtCysK Arabidopsis thaliana
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific, the C-terminal Ile (residue P4) is fundamental for the CysE/CysK binding interaction Mycobacterium tuberculosis
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific. The P4 Ile residue accounts for about 80% of total binding energy. The P2 and P3 positions account for about 10% each, and the P1 residue negatively impacts binding, interaction analysis Entamoeba histolytica
2.5.1.47 additional information each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific. The P4 Ile residue accounts for about 80% of total binding energy. The P2 and P3 positions account for about 10% each, and the P1 residue negatively impacts binding, interaction analysis. No negative cooperativity Haemophilus influenzae
2.5.1.47 physiological function CysK influences transcription in Caenorhabditis elegans. The enzyme from Caenorhabditis elegans interacts with EGL-9 in regulation of O2-dependent behavioral plasticity Caenorhabditis elegans
2.5.1.47 physiological function enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK Salmonella enterica subsp. enterica serovar Typhimurium
2.5.1.47 physiological function enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK Haemophilus influenzae
2.5.1.47 physiological function enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK Mycobacterium tuberculosis
2.5.1.47 physiological function enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK Entamoeba histolytica
2.5.1.47 physiological function enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. CysK influences transcription in Gram-positive bacteria. The enzyme from Staphylococcus aureus interacts with CymR in transcription repression Staphylococcus aureus
2.5.1.47 physiological function enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. Regulatory function of CysK/CysE interaction in plants, overview Arabidopsis thaliana
2.5.1.47 physiological function enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. Regulatory function of CysK/CysE interaction in plants, overview. Productive cysteine biosynthesis requires a high CysK to CysE ratio Glycine max
2.5.1.47 physiological function enzyme CysK is organized in a complex with serine acetyltransferase (CysE), which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. CysK also activates an antibacterial nuclease toxin produced by uropathogenic Escherichia coli. Role for CysK during bacterial contact-dependent growth inhibition involving the CDI system from uropathogenic Escherichi coli, overview. CysK-binding provides a mechanism to protect the bacterial CysE from cold-inactivation and proteolysis. Escherichia coli CysK acts as a so-called permissive factor to activate an antibacterial contact-dependent growth inhibition (CDI) toxin, and interacts with CdiA-CTUPEC536 in toxin activation Escherichia coli
2.5.1.47 physiological function enzyme CysK is organized in a complex with serine acetyltransferase (CysE), which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. CysK influences transcription in Gram-positive bacteria. In Bacillus subtilis, CysK modulates the affinity of an Rrf2-type transcription factor for its operator sequences, thereby regulating expression of the cysteine regulon. The enzyme from Bacillus subtilis interacts with CymR in transcription repression. CdiA-CT toxins are activated by CysK, also from other species Bacillus subtilis