Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
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- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,280 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline citrate Identifier CHEBI:16947 (Beilstein: 1884707; CAS: 126-44-3) help_outline Charge -3 Formula C6H5O7 InChIKeyhelp_outline KRKNYBCHXYNGOX-UHFFFAOYSA-K SMILEShelp_outline OC(CC([O-])=O)(CC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 31 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N5-[(S)-citryl]-D-ornithine Identifier CHEBI:142972 Charge -2 Formula C11H16N2O8 InChIKeyhelp_outline FFFKYGCGRTUBJH-KBUNVGBDSA-L SMILEShelp_outline [NH3+][C@@H](C([O-])=O)CCCNC(C[C@](CC([O-])=O)(C(=O)[O-])O)=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline AMP Identifier CHEBI:456215 Charge -2 Formula C10H12N5O7P InChIKeyhelp_outline UDMBCSSLTHHNCD-KQYNXXCUSA-L SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 508 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,129 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline staphyloferrin A Identifier CHEBI:142973 Charge -5 Formula C17H19N2O14 InChIKeyhelp_outline VJSIXUQLTJCRCS-DFQXCPINSA-I SMILEShelp_outline [C@](CC(N[C@@H](C([O-])=O)CCCNC(C[C@](CC([O-])=O)(C(=O)[O-])O)=O)=O)(CC([O-])=O)(O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:59140 | RHEA:59141 | RHEA:59142 | RHEA:59143 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Identification and characterization of the Staphylococcus aureus gene cluster coding for staphyloferrin A.
Cotton J.L., Tao J., Balibar C.J.
Siderophores are key virulence factors that allow bacteria to grow in iron-restricted environments. The Gram-positive pathogen Staphylococcus aureus is known to produce four siderophores for which genetic and/or structural data are unknown. Here we characterize the gene cluster responsible for pro ... >> More
Siderophores are key virulence factors that allow bacteria to grow in iron-restricted environments. The Gram-positive pathogen Staphylococcus aureus is known to produce four siderophores for which genetic and/or structural data are unknown. Here we characterize the gene cluster responsible for producing the prevalent siderophore staphyloferrin A. In addition to expressing the cluster in the heterologous host Escherichia coli, which confers the ability to synthesize the siderophore, we reconstituted staphyloferrin A biosynthesis in vitro by expressing and purifying two key enzymes in the pathway. As with other polycarboxylate siderophores, staphyloferrin A is biosynthesized using the recently described nonribosomal peptide synthetase independent siderophore (NIS) biosynthetic pathway. Two NIS synthetases condense two molecules of citric acid to d-ornithine in a stepwise ordered process with SfnaD using the delta-amine as a nucleophile to form the first amide followed by SfnaB utilizing the alpha-amine to complete staphyloferrin A synthesis. << Less
Biochemistry 48:1025-1035(2009) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.