Information on EC 6.3.2.26 - N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
6.3.2.26
-
RECOMMENDED NAME
GeneOntology No.
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O = 3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amid formation
-
-
-
-
peptide bond formation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
isopenicillin N biosynthesis
-
-
Metabolic pathways
-
-
Penicillin and cephalosporin biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
L-2-aminohexanedioate:L-cysteine:L-valine ligase (AMP-forming, valine-inverting)
Requires Mg2+. The enzyme contains 4'-phosphopantetheine, which may be involved in the mechanism of the reaction. Forms part of the penicillin biosynthesis pathway (for pathway, click here).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ACV synthetase
-
-
-
-
DELTA-(alpha-aminoadipyl)cysteinylvaline synthetase
-
-
-
-
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase
-
-
-
-
delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase
-
-
-
-
L-(alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase
-
-
-
-
L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase
-
-
-
-
synthetase, delta-(alpha-aminoadipyl)cysteinylvaline
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
57219-73-5
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Paecilomyces persicinus
-
-
-
Manually annotated by BRENDA team
a low penicillin production strain, gene pcbAB
UniProt
Manually annotated by BRENDA team
a low penicillin production strain, gene pcbAB, the strain contains a single copy of the penicillin gene cluster
UniProt
Manually annotated by BRENDA team
Penicillium chrysogenum Wisconsin 54-1255
a low penicillin production strain, gene pcbAB
UniProt
Manually annotated by BRENDA team
Penicillium chrysogenum Wisconsin 54-1255
a low penicillin production strain, gene pcbAB, the strain contains a single copy of the penicillin gene cluster
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
B6HLU1
RNAi-mediated silencing of penV gene, encoding protein Pc22g22150, UniProt-ID B6HTR9, provokes a drastic reduction of the production of the delta-(L-alpha-aminoadipyl-L-cysteinyl-D-valine) and isopenicillin N intermediates and the final product of the pathway
physiological function
B6HLU1
the enzyme catalyzes the non-ribosomal activation and condensation of the three constituent amino acids to form the tripeptide N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine, i.e. ACV
physiological function
Penicillium chrysogenum Wisconsin 54-1255
-
the enzyme catalyzes the non-ribosomal activation and condensation of the three constituent amino acids to form the tripeptide N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine, i.e. ACV
-
malfunction
Penicillium chrysogenum Wisconsin 54-1255
-
RNAi-mediated silencing of penV gene, encoding protein Pc22g22150, UniProt-ID B6HTR9, provokes a drastic reduction of the production of the delta-(L-alpha-aminoadipyl-L-cysteinyl-D-valine) and isopenicillin N intermediates and the final product of the pathway
-
additional information
B6HLU1
the ACVS is able to catalyse multiple activities including substrate amino acids adenylation, peptide-bond formation, epimerization and tripeptide release by an integrated thioesterase, since it contains three different modules each of approximately 1000 amino acids. The enzyme contains at least ten catalytic domains. The C-terminal region of ACVS bears the epimerase and the thioesterase domains and may be involved in the epimerization of LLL-ACV to LLD-ACV and in the hydrolysis of the thioester bond. Residues E3371, H3373, R3375 and E3376 belong to the epimerase active centre. Different fragments included in the C-terminal region of the enzyme control thioester hydrolysis. Role of the EGHGRE motif present in the epimerase domain of ACVS, the epimerization domain located in the third module (activating L-valine) contains seven partially conserved motifs E1 to E7, overview. The EGHGRE motif containing residues E3371, H3373, R3375 and E3376 is crucial for the activity of the ACVS, involvement of the GWSFG motif in the ACVS activity
additional information
Penicillium chrysogenum Wisconsin 54-1255
-
the ACVS is able to catalyse multiple activities including substrate amino acids adenylation, peptide-bond formation, epimerization and tripeptide release by an integrated thioesterase, since it contains three different modules each of approximately 1000 amino acids. The enzyme contains at least ten catalytic domains. The C-terminal region of ACVS bears the epimerase and the thioesterase domains and may be involved in the epimerization of LLL-ACV to LLD-ACV and in the hydrolysis of the thioester bond. Residues E3371, H3373, R3375 and E3376 belong to the epimerase active centre. Different fragments included in the C-terminal region of the enzyme control thioester hydrolysis. Role of the EGHGRE motif present in the epimerase domain of ACVS, the epimerization domain located in the third module (activating L-valine) contains seven partially conserved motifs E1 to E7, overview. The EGHGRE motif containing residues E3371, H3373, R3375 and E3376 is crucial for the activity of the ACVS, involvement of the GWSFG motif in the ACVS activity
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
show the reaction diagram
B6HLU1
-
-
-
?
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
show the reaction diagram
Penicillium chrysogenum Wisconsin 54-1255
B6HLU1
-
-
-
?
6-oxopiperidine 2-carboxylic acid + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
alpha-aminoadipic acid + L-valine + L-lysine + ?
L-delta-alpha-aminoadipyl-L-cysteinyl-D-valine + ?
show the reaction diagram
-
enzyme is a nonribosomal peptide synthetase (NRPS) able to form ribosome-independent peptide bonds
ACV
-
?
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
show the reaction diagram
Q5JIZ8
the enzyme is involved in coenzyme A biosynthesis in the archaea, strict preference for ATP. Among several amine substrates, activity is detected with beta-alanine, but not with gamma-aminobutyrate, glycine nor aspartate
-
-
?
DL-valine + L-O-(methylserine) + L-2-aminohexanedioate + ATP
L-O-(methylserinyl)-D-valine + L-O-(methylserinyl)-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
L-2-aminoadipate + allylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-allylglycinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
L-2-aminoadipate + L-cystathionine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
L-2-aminoadipate + L-cysteine + L-allo-isoleucine + ATP
L-delta-(aminoadipyl)-L-cysteinyl-D-allo-isoleucine + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
L-2-aminoadipate + L-cysteine + L-allo-isoleucine + ATP
L-delta-(aminoadipyl)-L-cysteinyl-D-allo-isoleucine + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
L-2-aminoadipate + L-cysteine + L-isoleucine + ATP
L-delta-(aminoadipyl)-L-cysteinyl-D-isoleucine + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
-
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
-
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
-
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
-
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
-
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
ir
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
Paecilomyces persicinus, Lysobacter lactamgenus
-
-
-
-
-
L-2-aminoadipate + L-homocysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-homocysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
L-2-aminoadipate + vinylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-vinylglycinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
S-carboxymethylcysteine + L-cysteine + L-valine + ATP
L-S-carboxymethylcysteinyl-L-cysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
S-carboxymethylcysteine + L-cysteine + L-valine + ATP
L-S-carboxymethylcysteinyl-L-cysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
L-glutamate + L-cysteine + L-valine + ATP
L-glutamyl-L-cysteinyl-D-valine + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
ACVSs are multifunctional enzymes that activate amino acids as aminoacyladenylates, forming a mixed anhydride with the a-phosphate group of ATP and releasing pyrophosphate, pure Streptomyces lactamdurans ACVS is able to activate alpha-aminoadipic acid or its lactam 6-oxopiperideine-2-carboxylic acid, a compound that is easily converted to alpha-aminoadipic acid, but is unable to use piperideine-6-carboxylate or pipecolic acid as substrates, enzyme is also able to use L-cystathionine with the same efficiency as L-cysteine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
show the reaction diagram
B6HLU1
-
-
-
?
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
show the reaction diagram
Penicillium chrysogenum Wisconsin 54-1255
B6HLU1
-
-
-
?
alpha-aminoadipic acid + L-valine + L-lysine + ?
L-delta-alpha-aminoadipyl-L-cysteinyl-D-valine + ?
show the reaction diagram
-
enzyme is a nonribosomal peptide synthetase (NRPS) able to form ribosome-independent peptide bonds
ACV
-
?
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
show the reaction diagram
Q5JIZ8
the enzyme is involved in coenzyme A biosynthesis in the archaea
-
-
?
additional information
?
-
-
ACVSs are multifunctional enzymes that activate amino acids as aminoacyladenylates, forming a mixed anhydride with the a-phosphate group of ATP and releasing pyrophosphate, pure Streptomyces lactamdurans ACVS is able to activate alpha-aminoadipic acid or its lactam 6-oxopiperideine-2-carboxylic acid, a compound that is easily converted to alpha-aminoadipic acid, but is unable to use piperideine-6-carboxylate or pipecolic acid as substrates, enzyme is also able to use L-cystathionine with the same efficiency as L-cysteine
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
optimal concentration: 1.5-5 mM
ATP
-
optimal concentration: 5 mM
ATP
-
ACVS has a adenylate-containing modules for ATP binding
ATP
B6HLU1
the non-ribosomal multidomain ACV synthetase requires ATP and Mg2+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
optimal concentration: 10 mM
Mg2+
-
optimal concentration: 10 mM
Mg2+
-
optimal concentration: 20 mM
Mg2+
B6HLU1
required
Mg2+
B6HLU1
the non-ribosomal multidomain ACV synthetase requires ATP and Mg2+
Mn2+
-
optimal concentration: 10 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-phosphopantoate
Q5JIZ8
substrate inhibition
5,5'-dithiobis-2-nitrobenzoate
-
1 mM
5,5'-dithiobis-2-nitrobenzoate
-
the major effect on ACVS activity is exerted by thiol-blocking agents, which almost completely inhibited the activity at 1 mM concentration, confirming the importance of thiol groups in ACVS activity
ATP
-
at concentrations about 5 mM
ATP
Q5JIZ8
substrate inhibition
bis-delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine
-
-
-
D-glucose
-
crude extract is inhibited due to deprivation of ATP via sugar metabolism
diphosphate
-
5 mM
dithiothreitol
-
-
glyceraldehyde-3-phosphate
-
reacts with L-cysteinee
iodoacetamide
-
1 mM
N-ethylmaleimide
-
1 mM
N-ethylmaleimide
-
the major effect on ACVS activity is exerted by thiol-blocking agents, which almost completely inhibited the activity at 1 mM concentration, confirming the importance of thiol groups in ACVS activity
phosphate
-
ACVS activity decreases 30% in the presence of 100 mM phosphate, being also affected by AMP and pyrophosphate, products of ATP hydrolysis
pyridoxal 5'-phosphate
-
2 mM
iodoacetamide
-
the major effect on ACVS activity is exerted by thiol-blocking agents, which almost completely inhibited the activity at 1 mM concentration, confirming the importance of thiol groups in ACVS activity
additional information
B6HLU1
PenV i.e. Pc22g22150 protein, located in the vacuolar membrane, affects drastically the biosynthesis of the ACV tripeptide and the beta-lactam pathway of Penicillium chrysogenum, overview
-
additional information
Q5JIZ8
feedback inhibition by CoA/acetyl-CoA and product inhibition by 4'-phosphopantothenate are not observed
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.16
(R)-4-phosphopantoate
Q5JIZ8
pH 6.5, 85C
2.44
ATP
Q5JIZ8
pH 6.5, 85C
0.34
beta-Alanine
Q5JIZ8
pH 6.5, 85C
0.045
L-aminoadipate
-
-
0.17
L-aminoadipate
-
-
0.63
L-aminoadipate
-
-
0.026
L-cysteine
-
-
0.08
L-cysteine
-
-
0.12
L-cysteine
-
-
0.08
L-valine
-
-
0.34
L-valine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.133
cysteine
-
under saturating conditions
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.38
Q5JIZ8
beta-alanine, pH 6.5, 85C
14.7
Q5JIZ8
ATP, pH 6.5, 85C
15.6
Q5JIZ8
(R)-4-phosphopantoate, pH 6.5, 85C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
-
in MOPS buffer
8.4
-
in Tris buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 8.5
-
optimal pH-range for ACVS
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
Q5JIZ8
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 95
Q5JIZ8
activity continues to increase with temperature elevation from 65C up to 95C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Thermococcus onnurineus (strain NA1)
Thermococcus onnurineus (strain NA1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
-
subunit of Streptomyces clavuligerus ACVS
700004
220000
-
gel filtration
440086
283000
-
subunit of Streptomyces clavuligerus ACVS
700004
404100
-
calculation from amino acid sequence
440085
404100
-
pcbAB gene from Nocardia lactamdurans is 10.9 kb long and encodes a 3649 amino acid ACVS
700004
411500
-
calculation from amino acid sequence
440085
414800
-
calculation from amino acid sequence
440085
422500
-
calculation from DNA-sequence, PAGE and gel filtration
440075
424100
-
calculation from amino acid sequence
440085
425000
-
gel filtration
440074
430000
-
gel filtration
440082
470000
-
gradient PAGE
440084
560000
-
monomer of Streptomyces clavuligerus ACVS that appears as a 500kDa band in SDS-PAGE
700004
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
-
ACVS from Streptomyces clavuligerus 2 subunits of 283 kDa and a subunit of 32 kDa
monomer
-
1 * 400000, SDS-PAGE
monomer
-
1 * 220000, SDS-PAGE
monomer
-
1 * 430000, SDS-PAGE
monomer
-
1 * 470000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
very unstable below pH 7
440081
8.5
-
very unstable above pH 8.5
440081
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
half of activity after 70 h
440081
25
-
half of activity after 10 h
440081
25
-
half of activity after 8 h
440083
32
-
half of activity after 10 min
440081, 440083
34
-
the mixture of ATP 5 mM, DDT 3 mM, Mg2+ 5 mM, aminoadipate 5 mM, cysteine 1 mM and valine 5 mM prevents the thermal inactivation, 91% activity after 10 min; the mixture of ATP 5 mM, Mg2+ 5 mM, valine 5 mM prevents the thermal inactivation, 92% activity after 10 min
440083
70
Q5JIZ8
6 h, no decrease in activity
727436
80
Q5JIZ8
half-life: 13.6 h
727436
90
Q5JIZ8
half-life: 8.2 h
727436
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol stabilizes enzyme activity
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dithiothreitol
-
8 mM leads to a 10% higher enzyme activity than at 3 mM
dithiothreitol
-
stability of crude enzyme is increased by dithiothreitol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, about 15% of activity after 10 months
-
-80C, no loss in activity after 6 weeks
-
-80C, several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ACVS of Streptomyces clavuligerus is purified 12fold using a combination of 2 successive chromatography steps on MonoQ columns separated by ultrafiltration; the recombinant of Streptomyces clavuligerus ACVS is purified from a Streptomyces lividans transformant 2785fold to near homogeneity by a combination of gel filtration, ultrafiltration, and ion-exchange chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ACVS of Streptomyces lactamdurans is produced as a recombinant protein from a Streptomyces lividans transformant, carrying the pcbAB gene
-
overexpression in Streptomyces lividans
-
expression in Escherichia coli
-
expression in Hansenula polymorpha, co-expression with Bacillus subtilis sfp gene encoding a phosphopantetheinyl transferase that activated ACVS
-
expression in Saccharomyces cerevisiae
-
gene pcbAB
B6HLU1
gene pcbAB, expression of plasmid p43gdh-ACVSthio encoding the sequence encoding the ACVS thiesterase gene domain, using the Aspergillus awamori gdh gene promoter plus the pcbAB gene transcriptional terminator, in Penicillium chrysogenum protoplasts
B6HLU1
overexpressed in Escherichoa coli
Q5JIZ8
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
B6HLU1
exchange of the conserved motifs 3371EGHGRE3376 (located in the putative epimerase domain) and 3629GWSFG3633 (located in the thioesterase domain) by site-directed-mutagenesis to LGFGLL and GWAFG, respectively, combined with deletion of the whole thioesterase domain (230 amino acids) and the different parts of this domain. The mutant enzymes show lower or null activity compared to the control strain
additional information
Penicillium chrysogenum Wisconsin 54-1255
-
exchange of the conserved motifs 3371EGHGRE3376 (located in the putative epimerase domain) and 3629GWSFG3633 (located in the thioesterase domain) by site-directed-mutagenesis to LGFGLL and GWAFG, respectively, combined with deletion of the whole thioesterase domain (230 amino acids) and the different parts of this domain. The mutant enzymes show lower or null activity compared to the control strain
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
production of beta-lactam antibiotics
medicine
-
production of penicillin