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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
-
?
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
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
additional information
?
-
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
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
-
-
-
-
?
S-carboxymethylcysteine + L-cysteine + L-valine + ATP
L-S-carboxymethylcysteinyl-L-cysteinyl-D-valine + AMP + diphosphate
-
-
-
-
?
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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4-phosphopantoate
substrate inhibition
5,5'-dithiobis-2-nitrobenzoate
bis-delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine
-
-
D-glucose
-
crude extract is inhibited due to deprivation of ATP via sugar metabolism
glyceraldehyde-3-phosphate
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
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
5,5'-dithiobis-2-nitrobenzoate
-
1 mM
ATP
-
at concentrations about 5 mM
glyceraldehyde
-
-
glyceraldehyde-3-phosphate
-
reacts with L-cysteinee
glyceraldehyde-3-phosphate
-
reacts with L-cysteinee
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
-
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
-
additional information
-
feedback inhibition by CoA/acetyl-CoA and product inhibition by 4'-phosphopantothenate are not observed
-
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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
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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ACVS_STRCL
805
0
88718
Swiss-Prot
-
ACVA_ACRCH
3712
0
414775
Swiss-Prot
other Location (Reliability: 1)
ACVA_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
3770
0
422502
Swiss-Prot
other Location (Reliability: 1)
ACVA_PENCH
3746
0
421076
Swiss-Prot
other Location (Reliability: 3)
ACVA_PENRW
Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255)
3746
0
421076
Swiss-Prot
other Location (Reliability: 3)
ACVS_AMYLA
3649
0
404088
Swiss-Prot
-
B8MM62_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
3939
0
437436
TrEMBL
other Location (Reliability: 1)
A0A077NVQ2_XENBV
1857
0
204376
TrEMBL
-
A0A238HBV2_9BURK
997
0
109619
TrEMBL
-
E3FPD1_STIAD
Stigmatella aurantiaca (strain DW4/3-1)
3678
0
405856
TrEMBL
-
Q3M5N6_TRIV2
Trichormus variabilis (strain ATCC 29413 / PCC 7937)
2033
0
227558
TrEMBL
-
B8M109_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
5091
0
566090
TrEMBL
other Location (Reliability: 2)
A0A077N8A5_XENBV
1857
0
204341
TrEMBL
-
A0A1N6MXM9_9GAMM
4584
0
509816
TrEMBL
-
A0A1N6MVX7_9GAMM
4400
0
491536
TrEMBL
-
B7PXZ1_IXOSC
342
0
38333
TrEMBL
other Location (Reliability: 2)
V5ZCZ5_9GAMM
2096
0
229653
TrEMBL
-
I2C685_BACAY
Bacillus amyloliquefaciens (strain Y2)
2568
0
289279
TrEMBL
-
I2C683_BACAY
Bacillus amyloliquefaciens (strain Y2)
1202
0
135342
TrEMBL
-
A0A7W9JYZ3_9XANT
3741
0
416444
TrEMBL
-
Q3MCQ0_TRIV2
Trichormus variabilis (strain ATCC 29413 / PCC 7937)
3498
0
392563
TrEMBL
-
A0A0N1G388_9ACTN
1882
0
203993
TrEMBL
-
B7P268_IXOSC
1561
0
169086
TrEMBL
other Location (Reliability: 1)
G0Q5C4_9ACTN
2570
0
266921
TrEMBL
-
D8G9C0_9CYAN
1362
0
153572
TrEMBL
-
A0A0N1G197_9ACTN
821
0
86710
TrEMBL
-
A0A411ZG70_9SPHN
568
1
61693
TrEMBL
-
I2CAP2_BACAY
Bacillus amyloliquefaciens (strain Y2)
875
0
100001
TrEMBL
-
A0A077PM67_XENBV
1830
0
201154
TrEMBL
-
A0A0F4YTD2_TALEM
5095
0
567789
TrEMBL
other Location (Reliability: 3)
A0A0F4FN20_RHIRD
492
0
54842
TrEMBL
-
G0PZX8_9ACTN
642
0
70170
TrEMBL
-
B8M4E7_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
5650
0
625696
TrEMBL
other Location (Reliability: 1)
G0Q141_9ACTN
2450
0
258639
TrEMBL
-
K9XML5_9CHRO
3699
0
415206
TrEMBL
-
I2C5E7_BACAY
Bacillus amyloliquefaciens (strain Y2)
1877
0
206163
TrEMBL
-
B8MC36_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2930
0
325964
TrEMBL
other Location (Reliability: 3)
A0A486XMR9_9GAMM
1147
0
128725
TrEMBL
-
V5Z9F5_9GAMM
1810
0
198789
TrEMBL
-
T2JZR3_CROWT
467
0
52489
TrEMBL
-
A0A031H697_9BURK
1344
0
145526
TrEMBL
-
Q0YRE5_9CHLB
414
0
47185
TrEMBL
-
M1QQW9_BACTU
1005
0
115168
TrEMBL
-
B8M2A8_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
3725
0
413131
TrEMBL
other Location (Reliability: 1)
A0A108UBG0_9GAMM
1117
0
122627
TrEMBL
-
A0A068QSH0_9GAMM
4941
0
544027
TrEMBL
-
A0A7U3Z3G3_9GAMM
3345
0
371556
TrEMBL
-
B8M8T3_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
5756
0
641259
TrEMBL
other Location (Reliability: 5)
B8MQ38_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2151
0
239511
TrEMBL
other Location (Reliability: 2)
B2IXJ7_NOSP7
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
4458
0
501165
TrEMBL
-
E2Q5R1_STRCL
3781
0
414738
TrEMBL
-
G8SBN4_ACTS5
Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110)
3540
0
377090
TrEMBL
-
D3VEI6_XENNA
Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 / AN6)
5994
0
665018
TrEMBL
-
W1J3Y2_9GAMM
1579
0
175754
TrEMBL
-
N1NG68_XENNE
3326
0
370713
TrEMBL
-
A0A0N1NKN2_9ACTN
3325
0
353714
TrEMBL
-
A0A7W9QI82_9XANT
3744
0
416473
TrEMBL
-
A0A073CET2_PLAAG
1598
0
180778
TrEMBL
-
D2PSM6_KRIFD
Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399)
472
0
51554
TrEMBL
-
I2C680_BACAY
Bacillus amyloliquefaciens (strain Y2)
1267
0
141885
TrEMBL
-
A0A0N1GRH5_9ACTN
2790
0
294881
TrEMBL
-
A0A563W4X2_9CYAN
2062
0
233322
TrEMBL
-
H0TRW6_9BRAD
1170
0
129444
TrEMBL
-
E5B8A5_ERWAM
1588
0
176613
TrEMBL
-
T2IYX3_CROWT
425
0
47771
TrEMBL
-
A0A7X6AU31_STRMQ
605
0
65241
TrEMBL
-
I2C681_BACAY
Bacillus amyloliquefaciens (strain Y2)
1194
0
134005
TrEMBL
-
A0A7U3YZ87_9GAMM
967
0
106389
TrEMBL
-
A0A7J0CC95_9ACTN
3720
0
411965
TrEMBL
-
D3V2X7_XENBS
Xenorhabdus bovienii (strain SS-2004)
8103
0
890502
TrEMBL
-
D3VIX9_XENNA
Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 / AN6)
3326
0
370760
TrEMBL
-
F6AUU8_DELSC
Delftia sp. (strain Cs1-4)
4316
0
467124
TrEMBL
-
A0A0B6XEI4_XENBV
8119
0
892062
TrEMBL
-
A0A1N6MWA1_9GAMM
4942
0
548099
TrEMBL
-
PPS_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
261
0
29845
Swiss-Prot
-
PPS_THEON
Thermococcus onnurineus (strain NA1)
261
0
29685
Swiss-Prot
-
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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, Acremonium persicinum, Amycolatopsis lactamdurans, Aspergillus nidulans, Lysobacter lactamgenus, 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