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Information on EC 2.3.1.164 - isopenicillin-N N-acyltransferase
for references in articles please use BRENDA:EC2.3.1.164
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.164 isopenicillin-N N-acyltransferase
IUBMB Comments
Proceeds by a two stage mechanism via 6-aminopenicillanic acid. Different from EC 3.5.1.11, penicillin amidase.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.3.1.164
- chrysogenum
- penicillium
-
pende
- aspergillus
- nidulans
-
phenylacetic
- phenylacetyl-coa
- beta-lactam
- benzylpenicillin
-
pcbab
- acremonium
- aa
-
delta-l-alpha-aminoadipyl-l-cysteinyl-d-valine
-
preprotein
- microbodies
-
cephalosporium
-
deacetylcephalosporin
- biotechnology
- synthesis
Reaction Schemes
showSynonyms
isopenicillin n acyltransferase, 6-aminopenicillanic acid acyltransferase, acyl coenzyme a:6-aminopenicillanic acid acyltransferase, acyl-coa:6-apa acyltransferase, ipn acyltransferase, acyl-coenzyme a:isopenicillin n acyltransferase, acyl-coa:isopenicillin n acyltransferase, isopenicillin-n n-acyltransferase, isopenicillin n:acyl coa acyltransferase, acyl-coenzyme a ipn acyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-aminopenicillanate acyltransferase
-
-
-
-
6-aminopenicillanic acid acyltransferase
-
-
-
-
6-aminopenicillinanic acid phenylacetyltransferase
-
-
-
-
6-aminopenicillinanic acylase
-
-
-
-
aatA
aatB
acyl coenzyme A:6-aminopenicillanic acid acyltransferase
-
-
-
-
acyl-CoA:6-aminopenicillanate acyltransferase
-
-
-
-
acyl-CoA:6-APA acyltransferase
-
-
-
-
acyl-CoA:isopenicillin N acyltransferase
-
-
-
-
acyl-coenzyme A:isopenicillin N acyltransferase
-
-
-
-
acyl-coenzyme A:isopenicillin N-acyltransferase
-
-
-
-
acyltransferase, 6-aminopenicillanate
-
-
-
-
IAT
isopenicillin N acyltransferase
isopenicillin N:acyl-CoA: acyltransferase
-
-
-
-
aatB
-
AN6775.3, gene encoding a penicillin V producing activity, which, in contrast to aatA, does not encode a peroxisomal targeting signal PTS1. aatB homologues also exist in non-penicillin-producing fungi and is suggested to be a paralogue of aatA.
isopenicillin N acyltransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phenylacetyl-CoA + isopenicillin N + H2O = CoA + penicillin G + L-2-aminohexanedioate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acylation
hydrolysis
Acylation
-
-
-
-
hydrolysis
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
penicillin K biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:isopenicillin N N-acyltransferase
Proceeds by a two stage mechanism via 6-aminopenicillanic acid. Different from EC 3.5.1.11, penicillin amidase.
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CAS REGISTRY NUMBER
COMMENTARY
54576-90-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phenoxyacetyl-CoA + isopenicillin N + H2O
CoA + penicillin V + L-2-aminohexanedioate
-
Substrates: -
Products: -
Products: -
?
phenoxyacetyl-CoA + isopenicillin N + H2O
CoA + penicillin V + L-2-aminohexanedioate
-
Substrates: -
Products: -
Products: -
?
phenylacetyl-CoA + 6-aminopenicillanic acid + H2O
CoA + benzylpenicillin
-
Substrates: -
Products: -
Products: -
?
phenylacetyl-CoA + 6-aminopenicillanic acid + H2O
CoA + benzylpenicillin
-
Substrates: acyl-CoA:6-aminopenicillanate acyltransferase activity
Products: -
Products: -
?
phenylacetyl-CoA + 6-aminopenicillanic acid + H2O
CoA + benzylpenicillin
-
Substrates: -
Products: -
Products: -
?
phenylacetyl-CoA + isopenicillin N + H2O
CoA + benzylpenicillin + L-2-aminohexanedioate
-
Substrates: -
Products: -
Products: -
?
phenylacetyl-CoA + isopenicillin N + H2O
CoA + benzylpenicillin + L-2-aminohexanedioate
-
Substrates: acyl-coenzyme A:isopenicillin N acyltransferase activity, S309 is involved in substrate acylation
Products: -
Products: -
?
phenylacetyl-CoA + isopenicillin N + H2O
CoA + penicillin G + L-2-aminohexanedioate
-
Substrates: -
Products: -
Products: -
?
phenylacetyl-CoA + isopenicillin N + H2O
CoA + penicillin G + L-2-aminohexanedioate
Substrates: -
Products: -
Products: -
?
phenylacetyl-CoA + isopenicillin N + H2O
CoA + penicillin G + L-2-aminohexanedioate
Substrates: IAT substitutes the alpha-aminoadipic acid side chain of isopenicillin N by a phenylacetic acid phenolate group from phenylacetyl-CoA
Products: -
Products: -
?
phenylacetyl-CoA + isopenicillin N + H2O
CoA + penicillin G + L-2-aminohexanedioate
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phenylacetyl-CoA + isopenicillin N + H2O
CoA + benzylpenicillin + L-2-aminohexanedioate
-
Substrates: -
Products: -
Products: -
?
phenylacetyl-CoA + isopenicillin N + H2O
CoA + penicillin G + L-2-aminohexanedioate
-
Substrates: -
Products: -
Products: -
?
phenylacetyl-CoA + isopenicillin N + H2O
CoA + penicillin G + L-2-aminohexanedioate
Substrates: -
Products: -
Products: -
?
phenylacetyl-CoA + isopenicillin N + H2O
CoA + penicillin G + L-2-aminohexanedioate
-
Substrates: -
Products: -
Products: -
?
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
C103A mutant enzyme which has lost its ability to be processed to the mature heterodimeric protein and thus represents the proenzyme form
-
-
brenda
Penicillium chrysogenum npe6 lacks isopenicillin N acyltransferase activity
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
the protein level of IAT already saturates at low cluster copy numbers, lack of correlation between the protein and transcript levels of the IAT enzyme
brenda
additional information
-
the protein level of IAT already saturates at low cluster copy numbers, lack of correlation between the protein and transcript levels of the IAT enzyme
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
IAT encoded by the aatB gene, lacking a peroxisomal targeting signal PTS1
brenda
-
IAT encoded by the aatA gene, containing a peroxisomal targeting signal PTS1
brenda
-
colocalization of isopenicillin N-acyltransferase and phenylacetyl-CoA ligase
brenda
-
colocalization of isopenicillin N-acyltransferase and phenylacetyl-CoA ligase
-
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
penicillin production in high-yielding strains can be further improved by the overexpression of IAT while at very high levels of IAT the precursor 6-aminopenicillic acid accumulates
malfunction
-
penicillin production in high-yielding strains can be further improved by the overexpression of IAT while at very high levels of IAT the precursor 6-aminopenicillic acid accumulates
-
metabolism
in the last step of penicillin biosynthesis, acyl-CoA:isopenicillin N acyltransferase catalyzes the conversion of isopenicillin N to penicillin G
physiological function
-
IAT catalyzes a limiting step in high-yielding penicillin production strains
physiological function
-
IAT catalyzes a limiting step in high-yielding penicillin production strains
-
additional information
substrate binding structure determined by homology modeling and molecular docking in different snapshots, and refined by molecular dynamic simulations. A site located in the region generated by beta1, beta2 and beta5 strands, which forms part of the central structure of beta-subunit, as the potential binding site of isopenicillin N, which establishes interactions with Cys103, Leu169, Gln172, Asp264, and Arg310, detailed overview
additional information
-
substrate binding structure determined by homology modeling and molecular docking in different snapshots, and refined by molecular dynamic simulations. A site located in the region generated by beta1, beta2 and beta5 strands, which forms part of the central structure of beta-subunit, as the potential binding site of isopenicillin N, which establishes interactions with Cys103, Leu169, Gln172, Asp264, and Arg310, detailed overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AATA_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
357
0
39236
Swiss-Prot
other Location (Reliability: 2)
AATA_PENCH
357
0
39939
Swiss-Prot
other Location (Reliability: 2)
AATA_PENRW
Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255)
357
0
39939
Swiss-Prot
other Location (Reliability: 2)
A0A0W8G4P3_9ZZZZ
366
1
39145
TrEMBL
other Location (Reliability: 3)
A0A8J5BVH8_9ASCO
383
0
41472
TrEMBL
other Location (Reliability: 2)
A4FKI9_SACEN
Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
358
0
37736
TrEMBL
-
A0A024HHE8_PSEKB
Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13)
359
0
38518
TrEMBL
-
A0A0P7XZ72_9RHOB
374
0
40755
TrEMBL
-
A0A8J5E4T3_9ASCO
381
0
41374
TrEMBL
other Location (Reliability: 2)
A0A2G9H6Z1_9LAMI
351
0
39132
TrEMBL
other Location (Reliability: 2)
A0A8J8W3J6_9EURO
362
0
39553
TrEMBL
Mitochondrion (Reliability: 4)
S0FW59_9DELT
348
0
39271
TrEMBL
-
A0A0T6AMV0_9BACT
120
0
13517
TrEMBL
-
A0A2P9HZH0_9ACTN
344
0
36470
TrEMBL
-
Q391H8_BURL3
Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383)
358
0
38562
TrEMBL
-
A0A484UEA3_9ZZZZ
362
0
38713
TrEMBL
Mitochondrion (Reliability: 3)
K0KNI2_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
394
0
44079
TrEMBL
other Location (Reliability: 3)
A0A484Q885_9ZZZZ
363
0
38886
TrEMBL
Mitochondrion (Reliability: 2)
A0A6J4UG33_9CHLR
372
0
40478
TrEMBL
-
A0A484QY80_9ZZZZ
363
0
38914
TrEMBL
Mitochondrion (Reliability: 2)
A0A085AGD5_9ENTR
368
0
40601
TrEMBL
-
A0A0P0RED0_9BURK
346
0
37862
TrEMBL
-
Q3HUS0_PENCH
357
0
39939
TrEMBL
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11000
29000
40000
11000
-
processed protein, subunit alpha, determined by SDS-PAGE and Western blot analysis
11000
-
alpha 1 * 11000 + beta 1 * 29000, derived from cleavage of the 40 kDa polypeptide, SDS-PAGE
11000
-
alpha 1 * 11000 + beta 1 * 29000, wild-type and recombinant enzyme, SDS-PAGE
29000
-
processed protein, subunit beta, determined by SDS-PAGE and Western blot analysis
29000
-
alpha 1 * 11000 + beta 1 * 29000, derived from cleavage of the 40 kDa polypeptide, SDS-PAGE
29000
-
alpha 1 * 11000 + beta 1 * 29000, wild-type and recombinant enzyme, SDS-PAGE
40000
-
unprocessed precursor polypeptide, proenzyme, SDS-PAGE
40000
-
isopenicillin N acyltransferase precursor, proacyltransferase, proIAT, determined by SDS-PAGE and Western blot analysis
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
recombinant expression in Hansenula polymorpha give a 40 kDa pre-protein that is processed into an 11 and 29 kDa subunit, SDS-PAGE
dimer
heterodimer
additional information
dimer
three-dimensional structure determined by homology modeling and molecular docking in different snapshots, and refined by molecular dynamic simulations, detailed overview. The gene for IAT, penDE, encodes a 357 residue proenzyme with a molecular weight of 40 kDa, which is processed autocatalytically to generate two polypeptides of 102 residues as alpha-subunit and 255 residues as beta-subunit
heterodimer
-
alpha 1 * 11000 + beta 1 * 29000, derived from cleavage of the 40 kDa polypeptide, SDS-PAGE
heterodimer
-
alpha 1 * 11000 + beta 1 * 29000, wild-type and recombinant enzyme, SDS-PAGE
additional information
-
isopenicillin N-acyltransferase and phenylacetyl-CoA ligase which supplies phenylacetic acid to the N-acyltransferase form a peroxisomal functional complex
additional information
-
isopenicillin N-acyltransferase and phenylacetyl-CoA ligase which supplies phenylacetic acid to the N-acyltransferase form a peroxisomal functional complex
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
additional information
-
ptoIAT overexpressed in Escherichia coli is not self-processed even when treated with Aspergillus nidulans crude extract
proteolytic modification
-
the intronless gene is expressed in Escherichia coli and self-processed efficiently into its alpha and beta subunits
proteolytic modification
-
recombinant expression in Hansenula polymorpha give a 40 kDa pre-protein that is processed into an 11 and 29 kDa subunit
proteolytic modification
the proenzyme is processed autocatalytically to generate two polypeptides forming alpha-subunit and beta-subunit
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, X-ray diffraction, monoclinic space group C2, unit-cell parameteres: a = 231.36 A, b = 68.27 A, c = 151.31 A, beta = 129.6° at -173°C
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C103S
-
unprocessed inactive variant of isopenicillin N acyltransferase
C103S or A or W
-
C103 is specifically required for recombinant proenzyme cleavage
S309A
-
recombinant proenzyme containing S309A is cleaved, however enzyme activity is not observed
additional information
additional information
-
disruption of the aatA gene reduces penicillin production to 20%, the remaining activity is attributed to the product of gene aatB
additional information
-
Overexpression of a mutated aatB-PTS1 gene in an aatA-disruption strain, leading to peroxisomal localization of AatB, increased the penicillin titre more than overexpression of the wild-type aatB.
additional information
-
in high-yielding penicillin production strains IAT is the limiting factor and that this limitation can be alleviated by a balanced overproduction of this enzyme. Cooverexpression of penDE with gene phl, encoding the phenylacetic acid CoA ligase leading to production of phenoxyacetyl-CoA and penicillin V
additional information
-
in high-yielding penicillin production strains IAT is the limiting factor and that this limitation can be alleviated by a balanced overproduction of this enzyme. Cooverexpression of penDE with gene phl, encoding the phenylacetic acid CoA ligase leading to production of phenoxyacetyl-CoA and penicillin V
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cell extracts of Penicillium chrysogenum are prepared, Escherichia coli soluble extracts are used for in vitro IAT activity measurement
-
recombinant wild-type enzyme with a C-terminal His-tag is purified in a single step using Ni2+ affinity chelate chromatography. A combination of 5 mM DTT + 250 mM NaCl + 5 mM EDTA is effective in preventing aggregation of the enzyme
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene penDE, lack of correlation between the protein and transcript levels of the IAT enzyme, quantitative real-time PCR expression analysis and gene copy number determination, overexpression of penDE in Penicillium chrysogenum strains DS47274, DS47273, and DS17690, introduction of penDE gene without introns into these strains in a random manner, via the nonhomologous end-joining pathway. Cooverexpression of penDE with gene phl, encoding the phenylacetic acid CoA ligase leading to production of phenoxyacetyl-CoA and penicillin V
-
overexpression in Escherichia coli, not self-processed even when treated with Aspergillus nidulans crude extract
-
pPenIAT and pPenIATC103S are used to express the penDE gene in Penicillium chrysogenum, pPBCalphabeta, pDEC103S and palphabeta-DEC103S are used for expression in Escherichia coli
-
the intronless gene is expressed in Escherichia coli and self-processed efficiently into its alpha and beta subunits
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of either 1,3-diaminopropane or spermidine leads to a rearrangement of the proteome resulting in an overrepresentation of enzymes involved in the biosynthesis of valine and other precursors (e.g. coenzyme A) of penicillin and to the overrepresentation of the last enzyme of the penicillin pathway, isopenicillin N acyltransferase
in strains overexpressing the genes encoding glyoxalase I and II, the protein levels of isopenicillin N synthase and isopenicillin N acyltransferase are increased
investigation of the intracellular proteomes of the Penicillium chrysogenum throughout pilot and industrial processes. The level of IPN acyltransferase at 80 h during the industrial process is around 2fold of that during the pilot process, indicating that the industrial process with a higher penicillin production per cell might provide available environments to induce overexpression of IPN acyltransferase and accelerate penicillin formation
transcription factor AnBH1 acting as a repressor of aatA and aatB expression
-
transcription factor AnCF acting as an activator of aatA and aatB expression
-
addition of either 1,3-diaminopropane or spermidine leads to a rearrangement of the proteome resulting in an overrepresentation of enzymes involved in the biosynthesis of valine and other precursors (e.g. coenzyme A) of penicillin and to the overrepresentation of the last enzyme of the penicillin pathway, isopenicillin N acyltransferase
addition of either 1,3-diaminopropane or spermidine leads to a rearrangement of the proteome resulting in an overrepresentation of enzymes involved in the biosynthesis of valine and other precursors (e.g. coenzyme A) of penicillin and to the overrepresentation of the last enzyme of the penicillin pathway, isopenicillin N acyltransferase
-
-
in strains overexpressing the genes encoding glyoxalase I and II, the protein levels of isopenicillin N synthase and isopenicillin N acyltransferase are increased
-
in strains overexpressing the genes encoding glyoxalase I and II, the protein levels of isopenicillin N synthase and isopenicillin N acyltransferase are increased
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
Penicillium chrysogenum npe6 lacking isopenicillin N acyltransferase activity is an excellent host for production of different beta-lactam antibiotics
synthesis
synthesis
-
strategy to improve penicillin biosynthesis by Penicillium chrysogenum by reducing reactive and toxic metabolic byproducts, 2-oxoaldehydes. This is achieved by overexpressing the genes encoding glyoxalase I and II, which results in a 10% increase in penicillin titers relative to the control strain. The protein levels of isopenicillin N synthase and isopenicillin N acyltransferase are increased in the glyoxalase transformants, whereas their transcript levels remains unaltered
synthesis
-
strategy to improve penicillin biosynthesis by Penicillium chrysogenum by reducing reactive and toxic metabolic byproducts, 2-oxoaldehydes. This is achieved by overexpressing the genes encoding glyoxalase I and II, which results in a 10% increase in penicillin titers relative to the control strain. The protein levels of isopenicillin N synthase and isopenicillin N acyltransferase are increased in the glyoxalase transformants, whereas their transcript levels remains unaltered
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tobin, M.B.; Baldwin, J.E.; Cole, S.C.J.; Miller, J.R.; Skatrud, P.L.; Sutherland, J.D.
The requirement for subunit interaction in the production of Penicillium chrysogenum acyl-coenzyme A:isopenicillin N acyltransferase in Escherichia coli
Gene
132
199-206
1993
Penicillium chrysogenum
brenda
Fernandez, F.J.; Gutierrez, S.; Velasco, J.; Montenegro, E.; Marcos, A.T.; Martin, J.F.
Molecular characterization of three loss-of-function mutations in the isopenicillin N-acyltransferase gene (penDE) of Penicillium chrysogenum
J. Bacteriol.
176
4941-4948
1994
Penicillium chrysogenum, Penicillium chrysogenum WIS 54-1255
brenda
Tobin, M.B.; Cole, S.C.J.; Kovacevic, S.; Miller, J.R.; Baldwin, J.E.; Sutherland, J.D.
Acyl-coenzyme A:isopenicillin N acyltransferase from Penicillium chrysogenum: effect of amino acid substitutions at Ser227, Ser230 and Ser309 on proenzyme cleavage and activity
FEMS Microbiol. Lett.
121
39-46
1994
Penicillium chrysogenum
brenda
Nielsen, J.; Jorgensen, H.S.
Metabolic control analysis of the penicillin biosynthetic pathway in a high-yielding strain of Penicillium chrysogenum
Biotechnol. Prog.
11
299-305
1995
Penicillium chrysogenum, Penicillium chrysogenum yielding
brenda
Tobin, M.B.; Cole, S.C.J.; Miller, J.R.; Baldwin, J.E.; Sutherland, J.D.
Amino-acid substitutions in the cleavage site of acyl-coenzyme A:isopenicillin N acyltransferase from Penicillium chrysogenum: effect on proenzyme cleavage and activity
Gene
162
29-35
1995
Penicillium chrysogenum
brenda
Hensgens, C.M.H.; Kroezinga, E.A.; van Montfort, B.A.; van der Laan, J.M.; Sutherland, J.D.; Dijkstra, B.W.
Purification, crystallization and preliminary x-ray diffraction of Cys103Ala acyl coenzyme A:isopenicillin N acyltransferase from Penicillium chrysogenum
Acta Crystallogr. Sect. D
58
716-718
2002
Penicillium chrysogenum
brenda
Fernandez, F.J.; Cardoza, R.E.; Montenegro, E.; Velasco, J.; Gutierrez, S.; Martin, J.F.
The isopenicillin N acyltransferases of Aspergillus nidulans and Penicillium chrysogenum differ in their ability to maintain the 40-kDa ab heterodimer in an undissociated form
Eur. J. Biochem.
270
1958-1968
2003
Aspergillus nidulans, Penicillium chrysogenum
brenda
Yoshida, H.; Hensgens, C.M.; van der Laan, J.M.; Sutherland, J.D.; Hart, D.J.; Dijkstra, B.W.
An approach to prevent aggregation during the purification and crystallization of wild type acyl coenzyme A: isopenicillin N acyltransferase from Penicillium chrysogenum
Protein Expr. Purif.
41
61-67
2005
Penicillium chrysogenum
brenda
Lamas-Maceiras, M.; Vaca, I.; Rodriguez, E.; Casqueiro, J.; Martin, J.F.
Amplification and disruption of the phenylacetyl-CoA ligase gene of Penicillium chrysogenum encoding an aryl-capping enzyme that supplies phenylacetic acid to the isopenicillin N acyltransferase
Biochem. J.
395
147-155
2005
Penicillium chrysogenum
brenda
Ullan, R.V.; Campoy, S.; Casqueiro, J.; Fernandez, F.J.; Martin, J.F.
Deacetylcephalosporin C production in Penicillium chrysogenum by expression of the isopenicillin N epimerization, ring expansion, and acetylation genes
Chem. Biol.
14
329-339
2007
Penicillium chrysogenum
brenda
Lutz, M.V.; Bovenberg, R.A.; van der Klei, I.J.; Veenhuis, M.
Synthesis of Penicillium chrysogenum acetyl-CoA:isopenicillin N acyltransferase in Hansenula polymorpha: first step towards the introduction of a new metabolic pathway
FEMS Yeast Res.
5
1063-1067
2005
Penicillium chrysogenum
brenda
Garcia-Estrada, C.; Vaca, I.; Fierro, F.; Sjollema, K.; Veenhuis, M.; Martin, J.F.
The unprocessed preprotein form IATC103S of the isopenicillin N acyltransferase is transported inside peroxisomes and regulates its self-processing
Fungal Genet. Biol.
45
1043-1052
2008
Penicillium chrysogenum
brenda
Kiel, J.A.; van den Berg, M.A.; Fusetti, F.; Poolman, B.; Bovenberg, R.A.; Veenhuis, M.; van der Klei, I.J.
Matching the proteome to the genome: the microbody of penicillin-producing Penicillium chrysogenum cells
Funct. Integr. Genomics
9
167-184
2009
Penicillium chrysogenum
brenda
Sproete, P.; Hynes, M.J.; Hortschansky, P.; Shelest, E.; Scharf, D.H.; Wolke, S.M.; Brakhage, A.A.
Identification of the novel penicillin biosynthesis gene aatB of Aspergillus nidulans and its putative evolutionary relationship to this fungal secondary metabolism gene cluster
Mol. Microbiol.
70
445-461
2008
Aspergillus n