Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
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- Name help_outline Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-β-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2} Identifier CHEBI:143773 Charge -4 Formula C42H42FeN3O26 InChIKeyhelp_outline TVPDLHGLFXAKQV-GYQOYKAHSA-G SMILEShelp_outline C1([C@H](CO)NC(=O)C2=C3C(=CC=C2)O[Fe-3]456(O3)OC7=C(C=C(C=C7O4)[C@H]8[C@@H]([C@H]([C@@H]([C@H](O8)CO)O)O)O)C(=O)N[C@H](C(OC[C@@H](C([O-])=O)NC(=O)C9=C(C(=CC(=C9)[C@H]%10[C@@H]([C@H]([C@@H]([C@H](O%10)CO)O)O)O)O5)O6)=O)CO1)=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 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 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline Fe(III)-[N-(C-5-[deoxy-β-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2 Identifier CHEBI:143776 Charge -2 Formula C32H35FeN2O21 InChIKeyhelp_outline GCFJENJKAKJHRU-YOSWHHHASA-I SMILEShelp_outline OC[C@H]1C(OC[C@@H](C([O-])=O)NC(=O)C2=C3C(=CC(=C2)[C@H]4[C@@H]([C@H]([C@@H]([C@H](O4)CO)O)O)O)O[Fe-]5(OC6=C(C=C(C=C6O5)[C@H]7[C@@H]([C@H]([C@@H]([C@H](O7)CO)O)O)O)C(=O)N1)O3)=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 N-(2,3-dihydroxybenzoyl)-L-serine Identifier CHEBI:58154 Charge -1 Formula C10H10NO6 InChIKeyhelp_outline VDTYHTVHFIIEIL-LURJTMIESA-M SMILEShelp_outline OC[C@H](NC(=O)c1cccc(O)c1O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:60396 | RHEA:60397 | RHEA:60398 | RHEA:60399 | |
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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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In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes.
Lin H., Fischbach M.A., Liu D.R., Walsh C.T.
The iroA locus encodes five genes (iroB, iroC, iroD, iroE, iroN) that are found in pathogenic Salmonella and Escherichia coli strains. We recently reported that IroB is an enterobactin (Ent) C-glucosyltransferase, converting the siderophore into mono-, di-, and triglucosyl enterobactins (MGE, DGE, ... >> More
The iroA locus encodes five genes (iroB, iroC, iroD, iroE, iroN) that are found in pathogenic Salmonella and Escherichia coli strains. We recently reported that IroB is an enterobactin (Ent) C-glucosyltransferase, converting the siderophore into mono-, di-, and triglucosyl enterobactins (MGE, DGE, and TGE, respectively). Here, we report the characterization of IroD and IroE as esterases for the apo and Fe(3+)-bound forms of Ent, MGE, DGE, and TGE, and we compare their activities with those of Fes, the previously characterized enterobactin esterase. IroD hydrolyzes both apo and Fe(3+)-bound siderophores distributively to generate DHB-Ser and/or Glc-DHB-Ser, with higher catalytic efficiencies (k(cat)/K(m)) on Fe(3+)-bound forms, suggesting that IroD is the ferric MGE/DGE esterase responsible for cytoplasmic iron release. Similarly, Fes hydrolyzes ferric Ent more efficiently than apo Ent, confirming Fes is the ferric Ent esterase responsible for Fe(3+) release from ferric Ent. Although each enzyme exhibits lower k(cat)'s processing ferric siderophores, dramatic decreases in K(m)'s for ferric siderophores result in increased catalytic efficiencies. The inability of Fes to efficiently hydrolyze ferric MGE, ferric DGE, or ferric TGE explains the requirement for IroD in the iroA cluster. IroE, in contrast, prefers apo siderophores as substrates and tends to hydrolyze the trilactone just once to produce linearized trimers. These data and the periplasmic location of IroE suggest that it hydrolyzes apo enterobactins while they are being exported. IroD hydrolyzes apo MGE (and DGE) regioselectively to give a single linear trimer product and a single linear dimer product as determined by NMR. << Less
J. Am. Chem. Soc. 127:11075-11084(2005) [PubMed] [EuropePMC]
This publication is cited by 9 other entries.