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Information on EC 6.3.2.26 - N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase
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6.3.2.26 N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthaseIUBMB Comments
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).
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Word Map
- 6.3.2.26
-
delta-l-alpha-aminoadipyl-l-cysteinyl-d-valine
- penicillin
- chrysogenum
- clavuligerus
- acremonium
- beta-lactams
- synthetases
- tripeptide
-
pcbab
- nidulans
-
cephalosporium
-
cephamycins
-
lld-acv
-
gramicidin
- pantoate
- kodakarensis
-
non-ribosomal
-
epimerization
-
l-alpha-aminoadipic
- 4'-phosphopantothenate
-
epsilon-aminotransferase
-
thiotemplate
-
tyrocidine
- medicine
- biotechnology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
ACV synthetase, ACVS, DELTA-(alpha-aminoadipyl)cysteinylvaline synthetase, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase, delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase, delta-(L-alpha-aminoadipyl-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, L-delta-alpha-aminoadipoyl-L-cysteinyl-D-valine synthetase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACV synthetase
ACVS
DELTA-(alpha-aminoadipyl)cysteinylvaline synthetase
-
-
-
-
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase
-
-
-
-
delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase
-
-
delta-(L-alpha-aminoadipyl-L-cysteinyl-D-valine synthetase)
delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase
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-
-
-
L-(alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase
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-
-
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L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase
-
-
-
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synthetase, delta-(alpha-aminoadipyl)cysteinylvaline
-
-
-
-
ACV synthetase
-
-
-
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delta-(L-alpha-aminoadipyl-L-cysteinyl-D-valine synthetase)
-
-
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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
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amid formation
-
-
-
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peptide bond formation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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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).
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CAS REGISTRY NUMBER
COMMENTARY
57219-73-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
6-oxopiperidine 2-carboxylic acid + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
-
-
-
?
alpha-aminoadipic acid + L-valine + L-lysine + ?
L-delta-alpha-aminoadipyl-L-cysteinyl-D-valine + ?
-
enzyme is a nonribosomal peptide synthetase (NRPS) able to form ribosome-independent peptide bonds
ACV
-
?
DL-valine + L-O-(methylserine) + L-2-aminohexanedioate + ATP
L-O-(methylserinyl)-D-valine + L-O-(methylserinyl)-D-valine + AMP + diphosphate
-
-
-
-
?
L-2-aminoadipate + allylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-allylglycinyl-D-valine + AMP + diphosphate
L-2-aminoadipate + L-cystathionine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
-
-
-
?
L-2-aminoadipate + L-cysteine + L-allo-isoleucine + ATP
L-delta-(aminoadipyl)-L-cysteinyl-D-allo-isoleucine + AMP + diphosphate
L-2-aminoadipate + L-cysteine + L-isoleucine + ATP
L-delta-(aminoadipyl)-L-cysteinyl-D-isoleucine + AMP + diphosphate
-
-
-
-
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
L-2-aminoadipate + L-homocysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-homocysteinyl-D-valine + AMP + diphosphate
-
-
-
-
?
L-2-aminoadipate + vinylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-vinylglycinyl-D-valine + AMP + diphosphate
L-glutamate + L-cysteine + L-valine + ATP
L-glutamyl-L-cysteinyl-D-valine + AMP + diphosphate
-
-
-
-
?
S-carboxymethylcysteine + L-cysteine + L-valine + ATP
L-S-carboxymethylcysteinyl-L-cysteinyl-D-valine + AMP + diphosphate
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
-
-
-
?
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
-
-
-
?
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
the enzyme is involved in coenzyme A biosynthesis in the archaea
-
-
?
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
strict preference for ATP. Among several amine substrates, activity is detected with beta-alanine, but not with gamma-aminobutyrate, glycine nor aspartate
-
-
?
L-2-aminoadipate + allylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-allylglycinyl-D-valine + AMP + diphosphate
-
-
-
-
?
L-2-aminoadipate + allylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-allylglycinyl-D-valine + AMP + diphosphate
-
-
-
-
?
L-2-aminoadipate + L-cysteine + L-allo-isoleucine + ATP
L-delta-(aminoadipyl)-L-cysteinyl-D-allo-isoleucine + AMP + diphosphate
-
-
-
-
?
L-2-aminoadipate + L-cysteine + L-allo-isoleucine + ATP
L-delta-(aminoadipyl)-L-cysteinyl-D-allo-isoleucine + AMP + diphosphate
-
-
-
-
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
-
-
-
-
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
-
-
-
-
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
-
-
-
-
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
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-
-
-
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L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
Paecilomyces persicinus
-
-
-
-
-
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
-
-
-
-
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
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-
-
-
-
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
-
-
-
ir
L-2-aminoadipate + vinylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-vinylglycinyl-D-valine + AMP + diphosphate
-
-
-
-
?
L-2-aminoadipate + vinylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-vinylglycinyl-D-valine + AMP + diphosphate
-
-
-
-
?
S-carboxymethylcysteine + L-cysteine + L-valine + ATP
L-S-carboxymethylcysteinyl-L-cysteinyl-D-valine + AMP + diphosphate
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-
-
-
?
S-carboxymethylcysteine + L-cysteine + L-valine + ATP
L-S-carboxymethylcysteinyl-L-cysteinyl-D-valine + AMP + diphosphate
-
-
-
-
?
additional information
?
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-
ACVSs are multifunctional enzymes that activate amino acids as aminoacyladenylates, forming a mixed anhydride with the a-phosphate group of ATP and releasing pyrophosphate
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-
-
additional information
?
-
-
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
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-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
alpha-aminoadipic acid + L-valine + L-lysine + ?
L-delta-alpha-aminoadipyl-L-cysteinyl-D-valine + ?
-
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
the enzyme is involved in coenzyme A biosynthesis in the archaea
-
-
?
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
-
-
-
?
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
-
-
-
?
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
-
-
-
additional information
?
-
-
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
the non-ribosomal multidomain ACV synthetase requires ATP and Mg2+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
the non-ribosomal multidomain ACV synthetase requires ATP and Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glucose
-
crude extract is inhibited due to deprivation of ATP via sugar metabolism
phosphate
-
ACVS activity decreases 30% in the presence of 100 mM phosphate, being also affected by AMP and pyrophosphate, products of ATP hydrolysis
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
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
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
additional information
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
feedback inhibition by CoA/acetyl-CoA and product inhibition by 4'-phosphopantothenate are not observed
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 95
activity continues to increase with temperature elevation from 65°C up to 95°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
a low penicillin production strain, gene pcbAB, the strain contains a single copy of the penicillin gene cluster
UniProt
brenda
a low penicillin production strain, gene pcbAB
UniProt
brenda
a low penicillin production strain, gene pcbAB, the strain contains a single copy of the penicillin gene cluster
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
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
malfunction
-
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
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
-
after heat shock, ACVS is singificantly upregulated. Phosphopantetheinyl transferase is coregulated with ACVS, confirming its role in activating ACVS. All components for L-alpha-aminoadipic acid synthesis are present and transcriptionally active in Folsomia candida
physiological function
-
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
-
additional information
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
-
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
ACVS_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
3770
0
422502
Swiss-Prot
A0A0F4YTD2_TALEM
5095
0
567789
TrEMBL
A0A0N1GRH5_9ACTN
2790
0
294881
TrEMBL
A0A073CET2_PLAAG
1598
0
180778
TrEMBL
D2PSM6_KRIFD
Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399)
472
0
51554
TrEMBL
D3VIX9_XENNA
Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6)
3326
0
370760
TrEMBL
A0A0N1NKN2_9ACTN
3325
0
353714
TrEMBL
A0A0N1G388_9ACTN
1882
0
203993
TrEMBL
B8M109_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
5091
0
566090
TrEMBL
B8MC36_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2930
0
325964
TrEMBL
A0A0A8P2V6_XENNE
3326
0
370838
TrEMBL
B8MQ38_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2151
0
239511
TrEMBL
M1QQW9_BACTU
1005
0
115168
TrEMBL
B8M8T3_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
5756
0
641259
TrEMBL
Q3M5N6_TRIV2
Trichormus variabilis (strain ATCC 29413 / PCC 7937)
2033
0
227558
TrEMBL
B2IXJ7_NOSP7
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
4458
0
501165
TrEMBL
E3FPD1_STIAD
Stigmatella aurantiaca (strain DW4/3-1)
3678
0
405856
TrEMBL
B8MM62_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
3939
0
437436
TrEMBL
A0A077N8A5_XENBV
1857
0
204341
TrEMBL
I2B0C4_FRANT
Francisella noatunensis subsp. orientalis (strain Toba 04)
2992
0
345161
TrEMBL
A0A077PM67_XENBV
1830
0
201154
TrEMBL
D3VEI6_XENNA
Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6)
5994
0
665018
TrEMBL
G8SBN4_ACTS5
Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110)
3540
0
377090
TrEMBL
B8M2A8_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
3725
0
413131
TrEMBL
B8M4E7_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
5650
0
625696
TrEMBL
B6HLU1_PENRW
Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255)
129
0
15409
TrEMBL
PPS_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
261
0
29845
Swiss-Prot
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Thermococcus onnurineus (strain NA1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
404100
560000
-
monomer of Streptomyces clavuligerus ACVS that appears as a 500kDa band in SDS-PAGE
404100
-
pcbAB gene from Nocardia lactamdurans is 10.9 kb long and encodes a 3649 amino acid ACVS
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
-
ACVS from Streptomyces clavuligerus 2 subunits of 283 kDa and a subunit of 32 kDa
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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
-
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
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dithiothreitol
dithiothreitol
-
8 mM leads to a 10% higher enzyme activity than at 3 mM
dithiothreitol
-
stability of crude enzyme is increased by dithiothreitol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ACVS of Streptomyces lactamdurans is produced as a recombinant protein from a Streptomyces lividans transformant, carrying the pcbAB gene
-
expression in Hansenula polymorpha, co-expression with Bacillus subtilis sfp gene encoding a phosphopantetheinyl transferase that activated ACVS
-
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kallow, W.; Neuhof, T.; Arezi, B.; Jungblut, P.; von Doehren, H.
Penicillin biosynthesis: intermediates of biosynthesis of delta-L-alpha-aminoadipyl-L-cysteinyl-D-valine formed by ACV synthetase from Acremonium chrysogenum
FEBS Lett.
414
74-78
1997
Acremonium chrysogenum
brenda
Kallow, W.; Von Dohren, H.; Kleinkauf, H.
Penicillin biosynthesis: energy requirement for tripeptide precursor formation by delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Acremonium chrysogenum
Biochemistry
37
5947-5952
1998
Acremonium chrysogenum
brenda
MacCabe, A.P.; Van Liempt, H.; Palissa, H.; Unkles, S.E.; Riach, M.B.R.; Pfeifer, E.; Von Doehren, H.; Kinghorn, J.R.
delta-(L-alpha-Aminoadipyl)-L-cysteinyl-D-valine synthetase from Aspergillus nidulans. Molecular characterization of the acvA gene encoding the first enzyme of the penicillin biosynthetic pathway
J. Biol. Chem.
266
12646-12654
1991
Aspergillus nidulans
brenda
Banko, G.; Demain, A.L.; Wolfe, S.
delta-(L-alpha-Aminoadipyl)-L-cysteinyl-D-valine synthetase (ACV synthetase): a multifunctional enzyme with broad substrate specificity for the synthesis of penicillin and cephalosporin precursors
J. Am. Chem. Soc.
109
2858-2860
1987
Acremonium chrysogenum
-
brenda
Baldwin, J.E.; Shiau, C.Y.; Byford, M.F.; Schofield, C.J.
Substrate specificity of L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase from Cephalosporium acremonium: demonstration of the structure of several unnatural tripeptide products
Biochem. J.
301
367-372
1994
Acremonium chrysogenum, Streptomyces clavuligerus
-
brenda
Zhang, J.; Demain, A.L.
Regulation of ACV synthetase activity in the beta-lactam biosynthetic pathway by carbon sources and their metabolites
Arch. Microbiol.
158
364-369
1992
Acremonium chrysogenum, Streptomyces clavuligerus
-
brenda
Shiau, C.Y.; Byford, M.F.; Baldwin, J.E.; Schofield, C.J.
Molecular mechanism of the multifunctional enzyme L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine (ACV) synthetase
Biochem. Soc. Trans.
23
629S
1995
Acremonium chrysogenum
brenda
Shiau, C.Y.; Byford, M.F.; Aplin, R.T.; Baldwin, J.E.; Schofield, C.J.
L-delta-(alpha-Aminoadipoyl)-L-cysteinyl-D-valine synthetase: thioesterification of valine is not obligatory for peptide bond formation
Biochemistry
36
8798-8806
1997
Acremonium chrysogenum
brenda
Zhang, J.; Wolfe, S.; Demain, A.L.
Biochemical studies on the activity of delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Streptomyces clavuligerus
Biochem. J.
283
691-698
1992
Streptomyces clavuligerus
brenda
Coque, J.J.R.; De la Fuente, J.L.; Liras, P.; Martin, J.F.
Overexpression of the Nocardia lactamdurans alpha-aminoadipyl-cysteinyl-valine synthetase in Streptomyces lividans. The purified multienzyme uses cystathionine and 6-oxopiperidine 2-carboxylate as substrates for synthesis of the tripeptide
Eur. J. Biochem.
242
264-270
1996
Amycolatopsis lactamdurans
brenda
Zhang, J.; Demain, A.L.
In vitro stabilization of ACV synthetase activity from Streptomyces clavuligerus
Appl. Biochem. Biotechnol.
37
97-110
1992
Streptomyces clavuligerus
-
brenda
Theilgaard, H.B.A.; Kristiansen, K.N.; Henriksen, C.M.; Nielsen, J.
Purification and characterization of delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Penicillium chrysogenum
Biochem. J.
327
185-191
1997
Penicillium chrysogenum
-
brenda
Aharonowitz, Y.; Bergmeyer, J.; Cantoral, J.M.; Cohen, G.; Demain, A.L.; Fink, U.; Kinghorn, J.; Kleinkauf, H.; MacCabe, A.; et al.
delta-(L-alpha-Aminoadipyl)-L-cysteinyl-D-valine synthetase, the multienzyme integrating the four primary reactions in b-lactam biosynthesis, as a model peptide synthetase
Bio/Technology
11
807-810
1993
Acremonium chrysogenum, Amycolatopsis lactamdurans, Aspergillus nidulans, Lysobacter lactamgenus, Paecilomyces persicinus, Penicillium chrysogenum
brenda
Byford, M.F.; Baldwin, J.E.; Shiau, C.Y.; Schofield, C.J.
The mechanism of ACV synthetase
Chem. Rev.
97
2631-2649
1997
Acremonium chrysogenum, Aspergillus nidulans, Penicillium chrysogenum, Streptomyces clavuligerus
brenda
Liras, P.; Demain, A.L.
Enzymology of beta-lactam compounds with cephem structure produced by actinomycete
Methods Enzymol.
458
401-429
2009
Actinomyces sp.
brenda
Siewers, V.; Chen, X.; Huang, L.; Zhang, J.; Nielsen, J.
Heterologous production of non-ribosomal peptide LLD-ACV in Saccharomyces cerevisiae
Metab. Eng.
11
391-397
2009
Penicillium chrysogenum
brenda
Gidijala, L.; Kiel, J.A.; Douma, R.D.; Seifar, R.M.; van Gulik, W.M.; Bovenberg, R.A.; Veenhuis, M.; van der Klei, I.J.
An engineered yeast efficiently secreting penicillin
PLoS ONE
4
e8317
2009
Penicillium chrysogenum
brenda
Fernandez-Aguado, M.; Teijeira, F.; Martin, J.F.; Ullan, R.V.
A vacuolar membrane protein affects drastically the biosynthesis of the ACV tripeptide and the beta-lactam pathway of Penicillium chrysogenum
Appl. Microbiol. Biotechnol.
97
795-808
2013
Penicillium chrysogenum (B6HLU1), Penicillium chrysogenum, Penicillium chrysogenum Wisconsin 54-1255 (B6HLU1)
brenda
Wu, X.; Garcia-Estrada, C.; Vaca, I.; Martin, J.F.
Motifs in the C-terminal region of the Penicillium chrysogenum ACV synthetase are essential for valine epimerization and processivity of tripeptide formation
Biochimie
94
354-364
2012
Penicillium chrysogenum (B6HLU1), Penicillium chrysogenum, Penicillium chrysogenum Wisconsin 54-1255 (B6HLU1)
brenda
Ishibashi, T.; Tomita, H.; Yokooji, Y.; Morikita, T.; Watanabe, B.; Hiratake, J.; Kishimoto, A.; Kita, A.; Miki, K.; Imanaka, T.; Atomi, H.
A detailed biochemical characterization of phosphopantothenate synthetase, a novel enzyme involved in coenzyme A biosynthesis in the Archaea
Extremophiles
16
819-828
2012
Thermococcus kodakarensis (Q5JIZ8), Thermococcus kodakarensis
brenda
Suring, W.; Marien, J.; Broekman, R.; van Straalen, N.M.; Roelofs, D.
Biochemical pathways supporting beta-lactam biosynthesis in the springtail Folsomia candida
Biol. Open
5
1784-1789
2016
Folsomia candida
brenda
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