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Literature summary for 6.3.2.26 extracted from
- Enzymology of beta-lactam compounds with cephem structure produced by actinomycete (2009), Methods Enzymol., 458, 401-429.
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | production of beta-lactam antibiotics | Actinomyces sp. |
Cloned(Commentary)
| 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
| 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 [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/ Products (Substrates)
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Actinomyces sp. | - |
- |
- |
Purification (Commentary)
| 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 and Products (Substrate)
| 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
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | ACVS from Streptomyces clavuligerus 2 subunits of 283 kDa and a subunit of 32 kDa | Actinomyces sp. |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ACV synthetase | - |
Actinomyces sp. |
| ACVS | - |
Actinomyces sp. |
| L-delta-alpha-aminoadipoyl-L-cysteinyl-D-valine synthetase | - |
Actinomyces sp. |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 8 | 8.5 | optimal pH-range for ACVS | Actinomyces sp. |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | ACVS has a adenylate-containing modules for ATP binding | Actinomyces sp. | |
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