Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.3.2.26 extracted from

  • 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 (2012), Biochimie, 94, 354-364.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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 Penicillium chrysogenum

Protein Variants

Protein Variants Comment Organism
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 Penicillium chrysogenum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the non-ribosomal multidomain ACV synthetase requires ATP and Mg2+ Penicillium chrysogenum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O Penicillium chrysogenum
-
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
-
?
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O Penicillium chrysogenum Wisconsin 54-1255
-
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
-
?

Organism

Organism UniProt Comment Textmining
Penicillium chrysogenum B6HLU1 a low penicillin production strain, gene pcbAB, the strain contains a single copy of the penicillin gene cluster
-
Penicillium chrysogenum Wisconsin 54-1255 B6HLU1 a low penicillin production strain, gene pcbAB, the strain contains a single copy of the penicillin gene cluster
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
-
Penicillium chrysogenum 3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
-
?
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
-
Penicillium chrysogenum Wisconsin 54-1255 3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
-
?

Synonyms

Synonyms Comment Organism
ACV synthetase
-
Penicillium chrysogenum
ACVS
-
Penicillium chrysogenum

Cofactor

Cofactor Comment Organism Structure
ATP the non-ribosomal multidomain ACV synthetase requires ATP and Mg2+ Penicillium chrysogenum

General Information

General Information Comment Organism
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 Penicillium chrysogenum