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Information on EC 2.3.1.175 - deacetylcephalosporin-C acetyltransferase and Organism(s) Acremonium chrysogenum and UniProt Accession P39058

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IUBMB Comments
This enzyme catalyses the final step in the biosynthesis of cephalosporin C.
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This record set is specific for:
Acremonium chrysogenum
UNIPROT: P39058
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The taxonomic range for the selected organisms is: Acremonium chrysogenum
The enzyme appears in selected viruses and cellular organisms
Synonyms
dcpc-atf, dac acetyltransferase, deacetylcephalosporin c acetyltransferase, dac-at, deacetylcephalosporin-c acetyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deacetylcephalosporin-C acetyltransferase
-
acetyl coenzyme A: deacetylacephalosporin C O-acetyltransferase
-
-
acetyl coenzyme A: deacetylcephalosporin C O-acetyltransferase
-
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acetyl coenzyme A:DAC acetyltransferase
-
-
acetyl-CoA:DAC acetyltransferase
-
-
acetyl-CoA:DAC O-acetyltransferase
-
-
acetyl-CoA:DAC-acetyltransferase
-
-
acetyl-CoA:deacetylcephalosporin C O-acetyltransferase
-
-
acetyl-CoA:deacetylcephalosporin-C acetyltransferase
-
-
CPC acetylhydrolase
-
-
DAC acetyltransferase
-
-
deacetylcephalosporin C acetyltransferase
-
-
deacetylcephalosporin-C acetyltransferase
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-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:deacetylcephalosporin-C O-acetyltransferase
This enzyme catalyses the final step in the biosynthesis of cephalosporin C.
CAS REGISTRY NUMBER
COMMENTARY hide
57827-76-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + deacetylcephalosporin C
CoA + cephalosporin C
show the reaction diagram
-
-
-
?
acetyl-CoA + deacetylcephalosporin C
CoA + cephalosporin C
show the reaction diagram
additional information
?
-
-
expression is regulated by methionine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + deacetylcephalosporin C
CoA + cephalosporin C
show the reaction diagram
-
-
-
?
acetyl-CoA + deacetylcephalosporin C
CoA + cephalosporin C
show the reaction diagram
additional information
?
-
-
expression is regulated by methionine
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,6-dihydroxybenzoic acid
-
0.1 mM, 27% inhibition
coenzyme A
-
0.1 mM, 61% inhibition
deacetoxycephalosporin C
-
0.1 mM, 57% inhibition
Penicillin N
-
0.1 mM, 14% inhibition
pyruvate
-
0.1 mM, 37% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 1.05
acetyl-CoA
0.04 - 0.29
deacetylcephalosporin C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25.8
-
deacetylcephalosporin-C acetyltransferase activity in the host strain Penicillium chrysogenum TA2
30
-
deacetylcephalosporin-C acetyltransferase activity in the host strain Penicillium chrysogenum TA98
6.7
-
deacetylcephalosporin-C acetyltransferase activity in the host strain Penicillium chrysogenum TA64
7.2
-
deacetylcephalosporin-C acetyltransferase activity in the host strain Penicillium chrysogenum TA71
additional information
-
0.0000378 mg cephalosporin C per min per mg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
no significant influence of pH-value on enzyme activity is measured after 20 min
7
-
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
-
pH 6.0: about 60% of maximal activity, pH 8.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
activity assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 40
-
15°C: about 45% of maximal activity, 40°C: about 75% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
chromatofocusing
4.3
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CEFG_ACRCH
444
0
49161
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
-
1 * 49000, SDS-PAGE
50000
-
gel filtration
55000
-
gel filtration
70000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
SDS-PAGE resolves two protein bands with molecular weights of 27000 Da and 14000 Da
monomer
-
1 * 49000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
DCPC-ATF is synthesized as a single-chain precursor protein and is then converted to the two constituent subunit DCPC-ATF by proteolytic processing
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
different structures are solved, SeMet-DAC-AT with acetyl-CoA to a resolution of 2.4 A, DAC-AT with acetyl-CoA to 2.2 A, DAC-AT with DAC/cephalosporin C to 2.5 A, and DAC-AT with DAC to 2.6 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using a gravity-flow column containing chitin beads, cleavage of the chitin-binding domain and intein fusion partner is performed
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the pTWIN vector for expression in Escherichia coli BL21DE3 cells
constructions starting at each of the three in-frame ATG codons of the Acremonium chrysogenum cefG gene (Met1, Met46 and Met60) are expressed in Escherichia coli, obtaining proteins of 49000 Da, 44000 Da and 43000 Da, respectively. All three proteins show deacetylcephalosporin C acetyltransferase activity, separately or in combination
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expression in Penicillium chrysogenum
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expression in yeast, the leader peptide is not essential for expression of the enzyme activity
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expression of the cefG gene from the promoters of 1. the glyceraldehyde-3-phosphate dehydrogenase gene of Aspergillus nidulans, 2. the glucoamylase gene of Aspergillus niger, 3. the glutamate dehydrogenase and 4. the isopenicillin N synthase genes of Penicillium chrysogenum, leads to very high steady-state levels of cefG transcript and to increased deacetylcephalosporin-C acetyltransferase protein concentration
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Penicillium chrysogenum strains expressing cefD1, cefD2, cefEF, and cefG genes cloned form Acremonium chrysogenum are constructed, deacetylcephalosporin-C acetyltransferase is coded by the cefG gene
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
studies of the enzyme will be useful in gaining a full view of the possibilities for overcoming the acetyl transfer bottleneck and for the future development of cephalosporin antibiotics
biotechnology
-
Penicillium chrysogenum npe6 lacking isopenicillin N acyltransferase activity is an excellent host for production of different beta-lactam antibiotics
synthesis
-
production of acetylcephalosporin C by gene expression in Penicillium chrysogenum. Recombinant strains secrete significant amounts of deacetylcephalosporin C, but acetylcephalosporin C is not detected in culture broth. Even when accumulating intracellularly, acetylcephalosporin C is not found extracellularly
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martin, J.F.; Gutierrez, S.; Fernandez, F.J.; Velasco, J.; Fierro, F.; Marcos, A.T.; Kosalkova, K.
Expression of genes and processing of enzymes for the biosynthesis of penicillins and cephalosporins
Antonie van Leeuwenhoek
65
227-243
1994
Acremonium chrysogenum
Manually annotated by BRENDA team
Gutierrez, S.; Velasco, J.; Marcos, A.T.; Fernandez, F.J.; Fierro, F.; Barredo, J.L.; Diez, B.; Martin, J.F.
Expression of the cefG gene is limiting for cephalosporin biosynthesis in Acremonium chrysogenum
Appl. Microbiol. Biotechnol.
48
606-614
1997
Acremonium chrysogenum
Manually annotated by BRENDA team
Matsuda, A.; Sugiura, H.; Matsuyama, K.; Matsumoto, H.; Ichikawa, S.; Komatsu, K.
Molecular cloning of acetyl coenzyme A: deacetylcephalosporin C O-acetyltransferase cDNA from Acremonium chrysogenum: sequence and expression of catalytic activity in yeast
Biochem. Biophys. Res. Commun.
182
995-1001
1992
Acremonium chrysogenum
Manually annotated by BRENDA team
Matsuda, A.; Sugiura, H.; Matsuyama, K.; Matsumoto, H.; Ichikawa, S.; Komatsu, K.
Cloning and disruption of the cefG gene encoding acetyl coenzyme A: deacetylcephalosporin C O-acetyltransferase from Acremonium chrysogenum
Biochem. Biophys. Res. Commun.
186
40-46
1992
Acremonium chrysogenum
Manually annotated by BRENDA team
Velasco, J.; Gutierrez, S.; Campoy, S.; Martin, J.F.
Molecular characterization of the Acremonium chrysogenum cefG gene product: the native deacetylcephalosporin C acetyltransferase is not processed into subunits
Biochem. J.
337
379-385
1999
Acremonium chrysogenum
Manually annotated by BRENDA team
Matsuyama, K.; Matsumoto, H.; Matsuda, A.; Sugiura, H.; Komatsu, K.; Ichikawa, S.
Purification of acetyl coenzyme A: deacetylacephalosporin C O-acetyltransferase from Acremonium chrysogenum
Biosci. Biotechnol. Biochem.
56
1410-1412
1992
Acremonium chrysogenum
Manually annotated by BRENDA team
Mathison, L.; Soliday, C.; Stepan, T.; Aldrich, T.; Rambosek, J.
Cloning, characterization, and use in strain improvement of the Cephalosporium acremonium gene cefG encoding acetyl transferase
Curr. Genet.
23
33-41
1993
Acremonium chrysogenum
Manually annotated by BRENDA team
Gutierrez, S.; Velasco, J.; Fernandez, F.J.; Martin, J.F.
The cefG gene of Cephalosporium acremonium is linked to the cefEF gene and encodes a deacetylcephalosporin C acetyltransferase closely related to homoserine O-acetyltransferase
J. Bacteriol.
174
3056-3064
1992
Acremonium chrysogenum
Manually annotated by BRENDA team
Scheidegger, A.; Gutzwiller, A.; Kuenzi, M.T.; Fiechter, A.; Nuesch, J.
Investigation of acetyl-CoA:deacetylcephalosporin C O-acetyltransferase of Cephalosporium acremonium
J. Biotechnol.
3
109-117
1985
Acremonium chrysogenum
-
Manually annotated by BRENDA team
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
Acremonium chrysogenum
Manually annotated by BRENDA team
Lejon, S.; Ellis, J.; Valegard, K.
The last step in cephalosporin C formation revealed: crystal structures of deacetylcephalosporin C acetyltransferase from Acremonium chrysogenum in complexes with reaction intermediates
J. Mol. Biol.
377
935-944
2008
Acremonium chrysogenum (P39058), Acremonium chrysogenum
Manually annotated by BRENDA team