Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	3 proteins
Enzyme class ^help_outline	EC 2.3.1.164 isopenicillin-N N-acyltransferase
GO Molecular Function ^help_outline	GO:0050640 isopenicillin-N N-acyltransferase activity

Reaction participants Show >> << Hide

Name ^help_outline H₂O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) ^help_outline Charge 0 Formula H2O InChIKey^help_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILES^help_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline isopenicillin N Identifier CHEBI:58399 Charge -1 Formula C14H20N3O6S InChIKey^help_outline MIFYHUACUWQUKT-GTQWGBSQSA-M SMILES^help_outline [H][C@]12SC(C)(C)[C@@H](N1C(=O)[C@H]2NC(=O)CCC[C@H]([NH3+])C([O-])=O)C([O-])=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 phenylacetyl-CoA Identifier CHEBI:57390 Charge -4 Formula C29H38N7O17P3S InChIKey^help_outline ZIGIFDRJFZYEEQ-CECATXLMSA-J SMILES^help_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)Cc1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline CoA Identifier CHEBI:57287 (Beilstein: 11604429) ^help_outline Charge -4 Formula C21H32N7O16P3S InChIKey^help_outline RGJOEKWQDUBAIZ-IBOSZNHHSA-J SMILES^help_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCS 2D coordinates Mol file for the small molecule Search links Involved in 1,500 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 InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_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 L-2-aminoadipate Identifier CHEBI:58672 Charge -1 Formula C6H10NO4 InChIKey^help_outline OYIFNHCXNCRBQI-BYPYZUCNSA-M SMILES^help_outline [NH3+][C@@H](CCCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline penicillin G Identifier CHEBI:51354 (Beilstein: 3915298) ^help_outline Charge -1 Formula C16H17N2O4S InChIKey^help_outline JGSARLDLIJGVTE-MBNYWOFBSA-M SMILES^help_outline [H][C@]12SC(C)(C)[C@@H](N1C(=O)[C@H]2NC(=O)Cc1ccccc1)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:20720	RHEA:20721	RHEA:20722	RHEA:20723
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	3 proteins	3 proteins
EC numbers ^help_outline	2.3.1.164
Gene Ontology ^help_outline	GO:0050640
KEGG ^help_outline				R04868
MetaCyc ^help_outline				2.3.1.164-RXN

Publications

Investigations into the post-translational modification and mechanism of isopenicillin N:acyl-CoA acyltransferase using electrospray mass spectrometry.

Aplin R.T., Baldwin J.E., Roach P.L., Robinson C.V., Schofield C.J.

Electrospray mass spectrometry (e.s.m.s.) was used to confirm the position of the post-translational cleavage of the isopenicillin N:acyl-CoA acyltransferase preprotein to give the alpha- and beta-subunits. The e.s.m.s. studies suggested partial modification of the alpha-subunit in vivo by exogeno ... >> More

Electrospray mass spectrometry (e.s.m.s.) was used to confirm the position of the post-translational cleavage of the isopenicillin N:acyl-CoA acyltransferase preprotein to give the alpha- and beta-subunits. The e.s.m.s. studies suggested partial modification of the alpha-subunit in vivo by exogenously added substituted acetic acids. E.s.m.s. has also allowed the observation in vitro of the transfer of the acyl group from several acyl-CoAs to the beta-subunit. N.m.r. data for the CoA species have been deposited as Supplementary Publication SUP 500173 (2 pages) at the British Library Document Supply Centre (DSC), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, from whom copies can be obtained on the terms indicated in Biochem. J. (1993) 289, 9. << Less

Biochem. J. 294:357-363(1993) [PubMed] [EuropePMC]
Molecular characterization of the acyl-coenzyme A:isopenicillin N acyltransferase gene (penDE) from Penicillium chrysogenum and Aspergillus nidulans and activity of recombinant enzyme in Escherichia coli.

Tobin M.B., Fleming M.D., Skatrud P.L., Miller J.R.

The final step in the biosynthesis of beta-lactam antibiotics in Penicillium chrysogenum and Aspergillus nidulans involves removal of the L-alpha-aminoadipyl side chain from isopenicillin N (IPN) and exchange with a nonpolar side chain. The enzyme catalyzing this reaction, acyl-coenzyme A:isopenic ... >> More

The final step in the biosynthesis of beta-lactam antibiotics in Penicillium chrysogenum and Aspergillus nidulans involves removal of the L-alpha-aminoadipyl side chain from isopenicillin N (IPN) and exchange with a nonpolar side chain. The enzyme catalyzing this reaction, acyl-coenzyme A:isopenicillin N acyltransferase (acyltransferase), was purified from P. chrysogenum and A. nidulans. Based on NH2-terminal amino acid sequence information, the acyltransferase gene (penDE) from P. chrysogenum and A. nidulans were cloned. In both organisms, penDE was located immediately downstream from the isopenicillin N synthetase gene (pcbC) and consisted of four exons encoding an enzyme of 357 amino acids (approximately 40 kilodaltons [kDa]). The DNA coding sequences showed approximately 73% identity, while the amino acid sequences were approximately 76% identical. Noncoding DNA regions (including the region between pcbC and penDE) were not conserved. Acyltransferase activity from Escherichia coli producing the 40-kDa protein accepted either 6-aminopenicillanic acid or IPN as the substrate and made a penicillinase-sensitive antibiotic in the presence of phenylacetyl coenzyme A. Therefore, a single gene is responsible for converting IPN to penicillin G. The active form of the enzyme may result from processing of the 40-kDa monomeric precursor to a heterodimer containing subunits of 11 and 29 kDa. << Less

J. Bacteriol. 172:5908-5914(1990) [PubMed] [EuropePMC]

RHEA:20720 H2O + isopenicillin N + phenylacetyl-CoA = CoA + H(+) + L-2-aminoadipate + penicillin G

Enzymes

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Cross-references

Publications

Investigations into the post-translational modification and mechanism of isopenicillin N:acyl-CoA acyltransferase using electrospray mass spectrometry.

Molecular characterization of the acyl-coenzyme A:isopenicillin N acyltransferase gene (penDE) from Penicillium chrysogenum and Aspergillus nidulans and activity of recombinant enzyme in Escherichia coli.