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IUBMB Comments Requires Mg2+ Staphylococcus aureus , catalyses the last step in the biosynthesis of the siderophore staphyloferrin B. It belongs to a class of siderophore synthases known as type B nonribosomal peptide synthase-independent synthases (NIS). Type B NIS enzymes recognize the δ-acid group of 2-oxoglutarate. The enzyme forms a 2-oxoglutarate adenylate intermediate prior to ligation.
Synonyms sbnC ,
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sbnC
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ATP + 2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate + L-2,3-diaminopropanoate = AMP + diphosphate + 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate
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MetaCyc
staphyloferrin B biosynthesis
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2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate:2-oxoglutarate ligase (staphyloferrin B-forming)
Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, catalyses the last step in the biosynthesis of the siderophore staphyloferrin B. It belongs to a class of siderophore synthases known as type B nonribosomal peptide synthase-independent synthases (NIS). Type B NIS enzymes recognize the delta-acid group of 2-oxoglutarate. The enzyme forms a 2-oxoglutarate adenylate intermediate prior to ligation.
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ATP + 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate + 2-oxoglutarate
AMP + diphosphate + staphyloferrin B
additional information
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Substrates: no activity with malate, glutarate, succinate, L-glutamate, and citrate
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ATP + 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate + 2-oxoglutarate
AMP + diphosphate + staphyloferrin B
Substrates: -
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ATP + 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate + 2-oxoglutarate
AMP + diphosphate + staphyloferrin B
Substrates: -
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ATP + 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate + 2-oxoglutarate
AMP + diphosphate + staphyloferrin B
Substrates: -
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ATP + 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate + 2-oxoglutarate
AMP + diphosphate + staphyloferrin B
ATP + 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate + 2-oxoglutarate
AMP + diphosphate + staphyloferrin B
Substrates: -
?
ATP + 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate + 2-oxoglutarate
AMP + diphosphate + staphyloferrin B
Substrates: -
?
ATP + 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate + 2-oxoglutarate
AMP + diphosphate + staphyloferrin B
Substrates: -
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Mg2+
0.25 mM used in assay conditions
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citrate
less than 20% residual activity at 2 mM. Citrate inhibits the enzyme by mimicking 2-oxoglutarate binding
malate
less than 50% residual activity at 2 mM
pyruvate
less than 80% residual activity at 2 mM
additional information
not inhibited by glutarate, succinate and L-glutamate
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0.324
2-oxoglutarate
at pH 7.5 and 25°C
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0.083
citrate
Staphylococcus aureus
at pH 7.5 and 25°C
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4.9
calculated from sequence
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UniProt
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
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physiological function
enzyme is involved in biosynthesis of staphyloferrin B. The SbnCEF synthetases and decarboxylase SbnH are necessary and sufficient to produce staphyloferrin B in vitro
physiological function
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enzyme is involved in biosynthesis of staphyloferrin B. The SbnCEF synthetases and decarboxylase SbnH are necessary and sufficient to produce staphyloferrin B in vitro
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SBNC_STAA8
Staphylococcus aureus (strain NCTC 8325 / PS 47)
584
0
66433
Swiss-Prot
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A0A389V6N4_STAAU
584
0
66406
TrEMBL
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additional information
enzyme exists as monomer and dimer, gel filtration
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dimer
and monomer, 2 * 66400, calculated from sequence
dimer
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and monomer, 2 * 66400, calculated from sequence
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monomer
and dimer, 1 * 66400, calculated from sequence
monomer
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and dimer, 1 * 66400, calculated from sequence
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selenomethionine-labeled enzyme, sitting drop vapor diffusion method, using 0.2 M trilithium citrate, 22% (w/v) PEG3350
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D344A
the mutant shows reduced activity compared to the wild type enzyme
E422A
the mutant shows severely reduced activity compared to the wild type enzyme
K552A
the mutant shows severely reduced activity compared to the wild type enzyme
L490A
the mutant shows strongly reduced activity compared to the wild type enzyme
R147A
the mutant shows severely reduced activity compared to the wild type enzyme
R297A
the mutant shows severely reduced activity compared to the wild type enzyme
R449A
the mutant shows strongly reduced activity compared to the wild type enzyme
R468A
the mutant shows strongly reduced activity compared to the wild type enzyme
Y298A
the mutant shows severely reduced activity compared to the wild type enzyme
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Ni-NTA column chromatography and Superdex 200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
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synthesis
the SbnCEF synthetases and decarboxylase SbnH are necessary and sufficient to produce staphyloferrin B in vitro in reactions containing component substrates L-2,3-diaminopropionic acid, citric acid and 2-oxoglutaric acid
synthesis
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the SbnCEF synthetases and decarboxylase SbnH are necessary and sufficient to produce staphyloferrin B in vitro in reactions containing component substrates L-2,3-diaminopropionic acid, citric acid and 2-oxoglutaric acid
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Cheung, J.; Beasley, F.C.; Liu, S.; Lajoie, G.A.; Heinrichs, D.E.
Molecular characterization of staphyloferrin B biosynthesis in Staphylococcus aureus
Mol. Microbiol.
74
594-608
2009
Staphylococcus aureus (Q2G1N1), Staphylococcus aureus NCTC 8325 (Q2G1N1)
brenda
Tang, J.; Ju, Y.; Zhou, J.; Guo, J.; Gu, Q.; Xu, J.; Zhou, H.
Structural and biochemical characterization of SbnC as a representative type B siderophore synthetase
ACS Chem. Biol.
15
2731-2740
2020
Staphylococcus aureus (A0A389V6N4)
brenda
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