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Information on EC 2.5.1.47 - cysteine synthase and Organism(s) Haemophilus influenzae and UniProt Accession P45040
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2.5.1.47 cysteine synthaseIUBMB Comments
A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (beta-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).
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Word Map
- 2.5.1.47
- h2s
- sulfur
- l-cysteine
- gsh
-
gamma-glutamyl
- acetyltransferase
- pyridoxal
-
slow-releasing
- typhimurium
- 5'-phosphate
-
gasotransmitter
-
o-acetylserinethiollyase
- nahs
- sulfite
-
gaseous
-
schiff
-
buthionine
- sulfoximine
- phytochelatins
-
assimilatory
-
plp-dependent
- desulfhydrase
-
h2s-releasing
- alpha-aminoacrylate
- thiosulfate
- oxygenase-1
- gamma-gcs
- sulphide
- dl-propargylglycine
-
transsulfuration
-
bienzyme
- 3-mercaptopyruvate
-
5'-phosphate-dependent
- beta-synthase
-
h2s-producing
-
sulfurylase
-
aldimine
-
beta-replacement
-
gamma-lyase
- sulfurtransferase
- cysb
- hydrosulfide
- biotechnology
- agriculture
- synthesis
- pharmacology
- medicine
- environmental protection
- drug development
- analysis
The taxonomic range for the selected organisms is: Haemophilus influenzae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
gyy4137, cysteine synthase, cysteine synthetase, o-acetylserine sulfhydrylase, oastl, oas-tl, o-acetylserine(thiol)lyase, csase, o-acetylserine (thiol) lyase, oass-a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylserine sulfhydrylase
-
-
-
-
CSase
-
-
-
-
cysteine synthetase
-
-
-
-
O-acetyl-L-serine acetate-lyase (adding hydrogen sulfide)
-
-
-
-
O-acetyl-L-serine sulfhydrylase
-
-
-
-
O-acetyl-L-serine sulfohydrolase
-
-
-
-
O-acetyl-L-serine(thiol)lyase
-
-
-
-
O-acetylserine (Thiol)-lyase
-
-
-
-
O-acetylserine (thiol)lyase
-
-
-
-
O-acetylserine sulfhydrylase
O-acetylserine sulfhydrylase A
-
-
-
-
O-acetylserine(thiol)lyase
-
-
-
-
O-acetylserine-O-acetylhomoserine sulfhydro-lyase
-
-
-
-
OAS Shase
-
-
-
-
OAS-TL
-
-
-
-
OASS
OASTL
-
-
-
-
S-sulfocysteine synthase
-
-
-
-
synthase, cysteine
-
-
-
-
O-acetylserine sulfhydrylase
-
-
-
-
O-acetylserine sulfhydrylase
-
cysteine synthase is a multiprotein assembly formed by the pyridoxal 5'-phosphate-dependent enzyme O-acetylserine sulfhydrylase and serine acetyltransferase
OASS
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
C-O bond cleavage
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (beta-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).
CAS REGISTRY NUMBER
COMMENTARY
37290-89-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
additional information
?
-
-
stopped-flow fluorescence spectroscopy is used to characterize the interaction of serine acetyltransferase with OASS and in the presence of the physiological regulators cysteine and bisulfide. Cysteine synthase assembly occurs via a two-step mechanism involving rapid formation of an encounter complex between the two enzymes, followed by a slow conformational change. The conformational change likely results from the closure of the active site of OASS upon binding of the serine acetyltransferase C-terminal peptide. Bisulfide stabilizes the cysteine synthase complex mainly by decreasing the back rate of the isomerization step. Cysteine, the product of the OASS reaction and a SAT inhibitor, slightly affects the kinetics of cysteine synthase formation leading to destabilization of the complex
-
-
?
additional information
?
-
-
the binding free energy of 400 pentapeptides, MNXXI, interacting with the HiOASS-A active site using a combined docking-scoring procedure based on GOLD and HINTare examined. The free energy prediction is verified by the experimental determination of the binding affinity of 14 of these pentapeptides, selected for spanning a large range of predicted binding affinity and presenting charged, polar, or apolar residues at mutation sites
-
-
?
additional information
?
-
the binding free energy of 400 pentapeptides, MNXXI, interacting with the HiOASS-A active site using a combined docking-scoring procedure based on GOLD and HINTare examined. The free energy prediction is verified by the experimental determination of the binding affinity of 14 of these pentapeptides, selected for spanning a large range of predicted binding affinity and presenting charged, polar, or apolar residues at mutation sites
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
additional information
?
-
-
stopped-flow fluorescence spectroscopy is used to characterize the interaction of serine acetyltransferase with OASS and in the presence of the physiological regulators cysteine and bisulfide. Cysteine synthase assembly occurs via a two-step mechanism involving rapid formation of an encounter complex between the two enzymes, followed by a slow conformational change. The conformational change likely results from the closure of the active site of OASS upon binding of the serine acetyltransferase C-terminal peptide. Bisulfide stabilizes the cysteine synthase complex mainly by decreasing the back rate of the isomerization step. Cysteine, the product of the OASS reaction and a SAT inhibitor, slightly affects the kinetics of cysteine synthase formation leading to destabilization of the complex
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
MNDGI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNEGI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNENI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNETI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNKGI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNKVI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNLGI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNPHI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNVPI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNWNI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNYFI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNYSI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
serine acetyltransferase
-
serine acetyltransferase (EC 2.3.1.30) can inhibit O-acetylserine sulfhydrylase catalytic activity with a double mechanism, the competition with O-acetylserine for binding to the enzyme active site and the stabilization of a closed conformation that is less accessible to the natural substrate
-
MNYDI
the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNYDI
interaction of the inhibitory pentapeptide MNYDI with CysK OASS isozyme from Salmonella typhimurium, the MNYDI peptide interacts with the HiCysK active site mainly through H-bonds involving its C-terminal carboxylate and hydrophobic interactions involving the side chains of Ile5 and Tyr3, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview
additional information
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
-
additional information
-
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
-
additional information
-
partial inhibition of enzyme upon complex formation with serine acetyltransferase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
important role of the C-terminal residue Ile5 and the arylic moiety at P3 in dictating enzyme affinity, dissociation constant of MNYDI
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.03
MNDGI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
2.27
MNEGI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.0387
MNENI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
3.42
MNETI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
15.2
MNKGI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
13.3
MNKVI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.57
MNLGI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.044
MNLNI
wild type serine acetyltransferase motif, 100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
7.1
MNPHI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
3.33
MNVPI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.0249
MNWNI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.0258
MNYDI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.191
MNYFI
100 mM HEPES, pH 8.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.0608
MNYSI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
malfunction
the inhibition of cysteine biosynthesis in prokaryotes and protozoa is proposed for the development of antibiotics
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
physiological function
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
physiological function
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complex with inhibitory pentapeptides MNYDI (10 mM HEPES, pH 8.0, 25 mM NaCl, 8.8 mM peptide), MNKGI (20 mM HEPES, pH 7.5, 20 mM NaCl, 12.5 mM peptide), MNWNI (10 mM HEPES, pH 7.5, 25 mM NaCl, 7.5 mM peptide), MNYFI (20 mM HEPES, pH 8.0, 20 mM NaCl, 12.7 mM peptide), MNENI (10 mM HEPES, pH 7.5, 25 mM NaCl, 9.4 mM peptide), and MNETI (20 mM HEPES, pH 7.5, 20 mM NaCl, 9.4 mM peptide), reservoir solution is 100 mM HEPES, pH 7.5, between 1.8 and 2.1 M (NH4)2SO4, and polyethylene glycol 400, except for the complex with MNWNI (100 mM CAPS, pH 10.5, 1.75 (NH4)2SO4, and 0.2 M Li2SO4), the cryoprotection solution contains glycerol, hanging drop vapor diffusion method, diffraction data are measured at -183°C
the X-ray structure of three (MNWNI, MNYDI, and MNENI) high affinity pentapeptide-OASS complexes are compared with the docked poses
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA affinity and Superdex 200 pg gel filtration chromatography
recombinant N-terminal His-tagged enzyme, cleavage and removal of the tag
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cysK, recombinant expression of N-terminal His-tagged enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
since mammals lack OASS, the enzyme is a potential target for antimicrobial agents
medicine
target for novel peptidomimetic antibiotics based on the C-terminal pentapeptide of serine acetyltransferase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, B.; Vetting, M.W.; Roderick, S.L.
The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase
J. Bacteriol.
187
3201-3205
2005
Haemophilus influenzae
Campanini, B.; Speroni, F.; Salsi, E.; Cook, P.F.; Roderick, S.L.; Huang, B.; Bettati, S.; Mozzarelli, A.
Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy
Protein Sci.
14
2115-2124
2005
Haemophilus influenzae
Salsi, E.; Campanini, B.; Bettati, S.; Raboni, S.; Roderick, S.L.; Cook, P.F.; Mozzarelli, A.
A two-step process controls the formation of the bienzyme cysteine synthase complex
J. Biol. Chem.
285
12813-12822
2010
Haemophilus influenzae
Salsi, E.; Bayden, A.S.; Spyrakis, F.; Amadasi, A.; Campanini, B.; Bettati, S.; Dodatko, T.; Cozzini, P.; Kellogg, G.E.; Cook, P.F.; Roderick, S.L.; Mozzarelli, A.
Design of O-acetylserine sulfhydrylase inhibitors by mimicking nature
J. Med. Chem.
53
345-356
2010
Haemophilus influenzae, Haemophilus influenzae (P45040)
Spyrakis, F.; Felici, P.; Bayden, A.S.; Salsi, E.; Miggiano, R.; Kellogg, G.E.; Cozzini, P.; Cook, P.F.; Mozzarelli, A.; Campanini, B.
Fine tuning of the active site modulates specificity in the interaction of O-acetylserine sulfhydrylase isozymes with serine acetyltransferase
Biochim. Biophys. Acta
1834
169-181
2013
Salmonella enterica (P0A1E3), Haemophilus influenzae (P45040), Haemophilus influenzae
Campanini, B.; Benoni, R.; Bettati, S.; Beck, C.M.; Hayes, C.S.; Mozzarelli, A.
Moonlighting O-acetylserine sulfhydrylase: new functions for an old protein
Biochim. Biophys. Acta
1854
1184-1193
2015
Arabidopsis thaliana (P47998), Bacillus subtilis (P37887), Caenorhabditis elegans (Q93244), Entamoeba histolytica (Q401L7), Escherichia coli (P0ABK5), Escherichia coli, Glycine max (A3RM03), Haemophilus influenzae (P45040), Mycobacterium tuberculosis (P9WP55), Salmonella enterica subsp. enterica serovar Typhimurium (P0A1E3), Staphylococcus aureus
Benoni, R.; Pertinhez, T.A.; Spyrakis, F.; Davalli, S.; Pellegrino, S.; Paredi, G.; Pezzotti, A.; Bettati, S.; Campanini, B.; Mozzarelli, A.
Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR
FEBS Lett.
590
943-953
2016
Salmonella enterica subsp. enterica serovar Typhimurium (P0A1E3), Salmonella enterica subsp. enterica serovar Typhimurium (P29848), Salmonella enterica subsp. enterica serovar Typhimurium, Haemophilus influenzae (P45040)
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