Application | Comment | Organism |
---|---|---|
biotechnology | production of beta-lactam antibiotics | Actinomyces sp. |
Cloned (Comment) | Organism |
---|---|
ACVS of Streptomyces lactamdurans is produced as a recombinant protein from a Streptomyces lividans transformant, carrying the pcbAB gene | Actinomyces sp. |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
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 | Actinomyces sp. | |
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 | Actinomyces sp. | |
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 | Actinomyces sp. | |
phosphate | ACVS activity decreases 30% in the presence of 100 mM phosphate, being also affected by AMP and pyrophosphate, products of ATP hydrolysis | Actinomyces sp. |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
32000 | - |
subunit of Streptomyces clavuligerus ACVS | Actinomyces sp. |
283000 | - |
subunit of Streptomyces clavuligerus ACVS | Actinomyces sp. |
404100 | - |
pcbAB gene from Nocardia lactamdurans is 10.9 kb long and encodes a 3649 amino acid ACVS | Actinomyces sp. |
560000 | - |
monomer of Streptomyces clavuligerus ACVS that appears as a 500kDa band in SDS-PAGE | Actinomyces sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-aminoadipic acid + L-valine + L-lysine + ? | Actinomyces sp. | enzyme is a nonribosomal peptide synthetase (NRPS) able to form ribosome-independent peptide bonds | L-delta-alpha-aminoadipyl-L-cysteinyl-D-valine + ? | ACV | ? | |
additional information | Actinomyces sp. | 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 | Actinomyces sp. | 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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Actinomyces sp. | - |
- |
- |
Purification (Comment) | Organism |
---|---|
ACVS of Streptomyces clavuligerus is purified 12fold using a combination of 2 successive chromatography steps on MonoQ columns separated by ultrafiltration | Actinomyces sp. |
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 | Actinomyces sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-aminoadipic acid + L-valine + L-lysine + ? | enzyme is a nonribosomal peptide synthetase (NRPS) able to form ribosome-independent peptide bonds | Actinomyces sp. | L-delta-alpha-aminoadipyl-L-cysteinyl-D-valine + ? | ACV | ? | |
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 | Actinomyces sp. | ? | - |
? | |
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 | Actinomyces sp. | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterodimer | ACVS from Streptomyces clavuligerus 2 subunits of 283 kDa and a subunit of 32 kDa | Actinomyces sp. |
Synonyms | Comment | Organism |
---|---|---|
ACV synthetase | - |
Actinomyces sp. |
ACVS | - |
Actinomyces sp. |
L-delta-alpha-aminoadipoyl-L-cysteinyl-D-valine synthetase | - |
Actinomyces sp. |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
8 | 8.5 | optimal pH-range for ACVS | Actinomyces sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | ACVS has a adenylate-containing modules for ATP binding | Actinomyces sp. |