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Literature summary for 1.3.99.36 extracted from

  • Ding, W.; Yuan, N.; Mandalapu, D.; Mo, T.; Dong, S.; Zhang, Q.
    Cypemycin decarboxylase CypD is not responsible for aminovinyl-cysteine (AviCys) ring formation (2018), Org. Lett., 20, 7670-7673 .
    View publication on PubMed
Search for more literature for 1.3.99.36

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys + acceptor Streptomyces coelicolor
-
 C3.19,S21-cyclocypemycin(1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide + CO2 + H2S + reduced acceptor
-
 ?
cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys + acceptor Streptomyces coelicolor M1414
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 C3.19,S21-cyclocypemycin(1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide + CO2 + H2S + reduced acceptor
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
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-
-
Streptomyces coelicolor M1414
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys + acceptor
-
 Streptomyces coelicolor C3.19,S21-cyclocypemycin(1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide + CO2 + H2S + reduced acceptor
-
 ?
cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys + acceptor
-
 Streptomyces coelicolor M1414 C3.19,S21-cyclocypemycin(1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide + CO2 + H2S + reduced acceptor
-
 ?
additional information cypemycin decarboxylase CypD is investigated by using a synthetic oligopeptide, which contains the to-becyclized dehydroalanine (Dha) residue. CypD efficiently catalyzes the decarboxylation of this Dha-containing peptide, but the expected AviCys ring is not formed in the product, suggesting that CypD alone is not enough to form the AviCys ring. The Dha-containing peptide is a better substrate than two similar peptides with a Ser or a Cys residue, supporting that, in cypemycin biosynthesis, Dha formation is prior to decarboxylation of the C-terminal Cys. The CypD-catalyzed decarboxylation is not coupled with AviCys ring formation. CypD alone is unable to form the AviCys ring. Production of Dha from the CypA Cys19 is likely prior to the CypD-catalyzed decarboxylation of Cys22 Streptomyces coelicolor ?
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additional information cypemycin decarboxylase CypD is investigated by using a synthetic oligopeptide, which contains the to-becyclized dehydroalanine (Dha) residue. CypD efficiently catalyzes the decarboxylation of this Dha-containing peptide, but the expected AviCys ring is not formed in the product, suggesting that CypD alone is not enough to form the AviCys ring. The Dha-containing peptide is a better substrate than two similar peptides with a Ser or a Cys residue, supporting that, in cypemycin biosynthesis, Dha formation is prior to decarboxylation of the C-terminal Cys. The CypD-catalyzed decarboxylation is not coupled with AviCys ring formation. CypD alone is unable to form the AviCys ring. Production of Dha from the CypA Cys19 is likely prior to the CypD-catalyzed decarboxylation of Cys22 Streptomyces coelicolor M1414 ?
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Synonyms

Synonyms Comment Organism
CYPD
-
 Streptomyces coelicolor
cypemycin decarboxylase
-
 Streptomyces coelicolor

Cofactor

Cofactor Comment Organism Structure
FAD dependent on Streptomyces coelicolor

General Information

General Information Comment Organism
additional information because only the C-terminal three residues of CypA are essential for CypD recognition, biochemical analyses in this study were performed by using synthetic oligopeptides. Since the C-terminal sequence of CypA is highly hydrophobic, we synthesized peptide 1 (KKSTISLVC) and peptide 2 (KKSTICLVC), which are similar to the CypA C-terminus but contain two Lys residues in the N-termini, to increase aqueous solubility and hence the reaction efficiency. Liquid chromatography coupled with high-resolution mass spectrometry (LC-HR-MS) analysis of each reaction mixture clearly show that both peptides are decarboxylated by CypD, suggesting that the two N-terminal Lys residues do not interfere with CypD activity Streptomyces coelicolor
physiological function ribosomally synthesized and post-translationally modified peptides (RiPPs) are a growing class of natural products that exist in all three domains of life and possess diverse biological activities. -RiPPs are derived from a ribosomally synthesized precursor peptide, which, in most cases, consists of an N-terminal region (leader peptide) that is essential for the recognition by post-translationally modifying enzymes, and a C-terminal region (core peptide) that is finally transformed to the mature product. A unique RiPP structural motif is S-[(Z)-2-aminovinyl]-D-cysteine (AviCys) has been found in several classes of RiPPs. Cypemycin decarboxylase (CypD) catalyzes the the AviCys formation. In cypemycin biosynthesis, Dha formation is prior to decarboxylation of the C-terminal Cys. AviCys is structurally similar to lanthionine, a characteristic motif that defines lanthipeptides (lanthionine-containing peptides). Cypemycin decarboxylase CypD is not responsible for aminovinyl-cysteine (AviCys) ring formation. AviCys formation does not require a specific cyclase. It is proposed that the AviCys motif may be produced enzymatically by feeding the Dha-containing peptide substrate to the corresponding decarboxylase. Cypemycin is a prototypical member of the linaridin family, which is defined as linear dehydrated (arid) peptides. CypD alone is unable to form the AviCys ring. Production of Dha from the CypA Cys19 is likely prior to the CypD-catalyzed decarboxylation of Cys22 Streptomyces coelicolor