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IUBMB Comments Requires Mg2+ Staphylococcus aureus , catalyses the last step in the biosynthesis of the siderophore staphyloferrin A. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme forms a citrate adenylate intermediate prior to ligation.
6.3.2.57
aspiration
needle
fine-needle
lymphoma
ultrasound
hodgkin
cytologic
splenic
suspicious
22-gauge
mammographic
splenectomy
non-hodgkin
metaplasia
non-invasive
putida
acyl-coa
postoperative
splenomegaly
hyperplasia
sigma54-dependent
Synonyms
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sfaBD
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sfnaB
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ATP + N5-[(S)-citryl]-D-ornithine + citrate = AMP + diphosphate + staphyloferrin A
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MetaCyc
staphyloferrin A biosynthesis
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N5-[(S)-citryl]-D-ornithine:citrate ligase (staphyloferrin A-forming)
Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, catalyses the last step in the biosynthesis of the siderophore staphyloferrin A. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme forms a citrate adenylate intermediate prior to ligation.
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ATP + N5-[(S)-citryl]-D-ornithine + citrate
AMP + diphosphate + staphyloferrin A
ATP + N5-[(S)-citryl]-D-ornithine + citrate
AMP + diphosphate + staphyloferrin A
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Substrates: -
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ATP + N5-[(S)-citryl]-D-ornithine + citrate
AMP + diphosphate + staphyloferrin A
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Substrates: -
?
ATP + N5-[(S)-citryl]-D-ornithine + citrate
AMP + diphosphate + staphyloferrin A
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Substrates: -
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ATP + N5-[(S)-citryl]-D-ornithine + citrate
AMP + diphosphate + staphyloferrin A
ATP + N5-[(S)-citryl]-D-ornithine + citrate
AMP + diphosphate + staphyloferrin A
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Substrates: -
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ATP + N5-[(S)-citryl]-D-ornithine + citrate
AMP + diphosphate + staphyloferrin A
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Substrates: -
?
ATP + N5-[(S)-citryl]-D-ornithine + citrate
AMP + diphosphate + staphyloferrin A
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Substrates: -
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Adenocarcinoma
Distinction between postsurgical changes and carcinoma by means of stereotaxic fine-needle aspiration biopsy after reduction mammaplasty.
Carcinoma
Pre-operative simultaneous stereotactic core biopsy and fine-needle aspiration biopsy in the diagnosis of invasive lobular breast carcinoma.
Histiocytic Sarcoma
Fine needle aspiration biopsy of the spleen. A useful procedure in the diagnosis of splenomegaly.
Leukemia
Fine needle aspiration biopsy of the spleen. A useful procedure in the diagnosis of splenomegaly.
Lymphoma
Fine needle aspiration biopsy of the spleen. A useful procedure in the diagnosis of splenomegaly.
Myeloproliferative Disorders
Fine-needle aspiration biopsy and flow cytometry immunophenotyping of lymphoid and myeloproliferative disorders of the spleen.
Neoplasms
Fine needle aspiration biopsy of the spleen. A useful procedure in the diagnosis of splenomegaly.
Starvation
Transcriptional regulation of the sulfate-starvation-induced gene sfnA by a sigma54-dependent activator of Pseudomonas putida.
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brenda
Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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SFNAB_STAA8
Staphylococcus aureus (strain NCTC 8325 / PS 47)
585
0
67211
Swiss-Prot
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x * 67200, SDS-PAGE
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x * 67200, SDS-PAGE
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Talon metal affinity column chromatography
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expressed in Escherichia coli BL21(DE3) cells
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the enzyme activity is inhibited in Staphylococcus aureus during glycolytic growth
the enzyme activity is inhibited in Staphylococcus aureus during glycolytic growth
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the enzyme activity is inhibited in Staphylococcus aureus during glycolytic growth
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Sheldon, J.R.; Marolda, C.L.; Heinrichs, D.E.
TCA cycle activity in Staphylococcus aureus is essential for iron-regulated synthesis of staphyloferrin A, but not staphyloferrin B: the benefit of a second citrate synthase
Mol. Microbiol.
92
824-839
2014
Staphylococcus aureus
brenda
Cotton, J.L.; Tao, J.; Balibar, C.J.
Identification and characterization of the Staphylococcus aureus gene cluster coding for staphyloferrin A
Biochemistry
48
1025-1035
2009
Staphylococcus aureus
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