EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
6.3.2.26 | DL-valine + L-O-(methylserine) + L-2-aminohexanedioate + ATP |
- |
Acremonium chrysogenum |
L-O-(methylserinyl)-D-valine + L-O-(methylserinyl)-D-valine + AMP + diphosphate |
- |
? |
6.3.2.26 | L-2-aminoadipate + allylglycine + L-valine + ATP |
- |
Acremonium chrysogenum |
L-delta-(aminoadipyl)-L-allylglycinyl-D-valine + AMP + diphosphate |
- |
? |
6.3.2.26 | L-2-aminoadipate + L-cysteine + L-allo-isoleucine + ATP |
- |
Acremonium chrysogenum |
L-delta-(aminoadipyl)-L-cysteinyl-D-allo-isoleucine + AMP + diphosphate |
- |
? |
6.3.2.26 | L-2-aminoadipate + L-cysteine + L-valine + ATP |
- |
Acremonium chrysogenum |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate |
- |
? |
6.3.2.26 | L-2-aminoadipate + vinylglycine + L-valine + ATP |
- |
Acremonium chrysogenum |
L-delta-(aminoadipyl)-L-vinylglycinyl-D-valine + AMP + diphosphate |
- |
? |
6.3.2.26 | S-carboxymethylcysteine + L-cysteine + L-valine + ATP |
- |
Acremonium chrysogenum |
L-S-carboxymethylcysteinyl-L-cysteinyl-D-valine + AMP + diphosphate |
- |
? |
6.3.2.26 | L-2-aminoadipate + L-cysteine + L-valine + ATP |
- |
Acremonium persicinum |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate |
- |
? |
6.3.2.26 | 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 |
? |
6.3.2.26 | more |
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. |
? |
- |
? |
6.3.2.26 | more |
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. |
? |
- |
? |