Enzymes
| UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
- Name help_outline 4-amino-L-phenylalanine Identifier CHEBI:143072 Charge 0 Formula C9H12N2O2 InChIKeyhelp_outline CMUHFUGDYMFHEI-QMMMGPOBSA-N SMILEShelp_outline C1=CC(=CC=C1C[C@@H](C([O-])=O)[NH3+])N 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
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Namehelp_outline
holo-[peptidyl-carrier protein]
Identifier
RHEA-COMP:11480
Reactive part
help_outline
- Name help_outline O-(pantetheine-4ʼ-phosphoryl)-L-serine residue Identifier CHEBI:64479 Charge -1 Formula C14H25N3O8PS SMILEShelp_outline C(NC(CCNC(=O)[C@@H](C(COP(OC[C@@H](C(*)=O)N*)(=O)[O-])(C)C)O)=O)CS 2D coordinates Mol file for the small molecule Search links Involved in 207 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- 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 1,328 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
4-amino-L-phenylalanyl-[peptidyl-carrier protein]
Identifier
RHEA-COMP:15237
Reactive part
help_outline
- Name help_outline O-(S-4-amino-L-phenylalanylpantetheine-4'-phosphoryl)serine residue Identifier CHEBI:142855 Charge 0 Formula C23H36N5O9PS SMILEShelp_outline C(=O)([C@@H]([NH3+])CC1=CC=C(C=C1)N)SCCNC(CCNC(=O)[C@@H](C(COP(OC[C@@H](C(*)=O)N*)(=O)[O-])(C)C)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 529 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 1,188 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:59436 | RHEA:59437 | RHEA:59438 | RHEA:59439 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| MetaCyc help_outline |
Publications
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Structure of a dinuclear iron cluster-containing beta-hydroxylase active in antibiotic biosynthesis.
Makris T.M., Knoot C.J., Wilmot C.M., Lipscomb J.D.
A family of dinuclear iron cluster-containing oxygenases that catalyze β-hydroxylation tailoring reactions in natural product biosynthesis by nonribosomal peptide synthetase (NRPS) systems was recently described [Makris, T. M., Chakrabarti, M., Münck, E., and Lipscomb, J. D. (2010) Proc. Natl. Aca ... >> More
A family of dinuclear iron cluster-containing oxygenases that catalyze β-hydroxylation tailoring reactions in natural product biosynthesis by nonribosomal peptide synthetase (NRPS) systems was recently described [Makris, T. M., Chakrabarti, M., Münck, E., and Lipscomb, J. D. (2010) Proc. Natl. Acad. Sci. U.S.A. 107, 15391-15396]. Here, the 2.17 Å X-ray crystal structure of the archetypal enzyme from the family, CmlA, is reported. CmlA catalyzes β-hydroxylation of l-p-aminophenylalanine during chloramphenicol biosynthesis. The fold of the N-terminal domain of CmlA is unlike any previously reported, but the C-terminal domain has the αββα fold of the metallo-β-lactamase (MBL) superfamily. The diiron cluster bound in the C-terminal domain is coordinated by an acetate, three His residues, two Asp residues, one Glu residue, and a bridging oxo moiety. One of the Asp ligands forms an unusual monodentate bridge. No other oxygen-activating diiron enzyme utilizes this ligation or the MBL protein fold. The N-terminal domain facilitates dimerization, but using computational docking and a sequence-based structural comparison to homologues, we hypothesize that it likely serves additional roles in NRPS recognition and the regulation of O2 activation. << Less
Biochemistry 52:6662-6671(2013) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Formation of an aminoacyl-S-enzyme intermediate is a key step in the biosynthesis of chloramphenicol.
Pacholec M., Sello J.K., Walsh C.T., Thomas M.G.
Herein we report the first biochemical characterization of an enzyme involved in the biosynthesis of chloramphenicol that provides new insights into the origins of the antibiotic.