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Literature summary for 1.3.99.36 extracted from

  • Ding, W.; Mo, T.; Mandalapu, D.; Zhang, Q.
    Substrate specificity of the cypemycin decarboxylase CypD (2018), Synth. Syst. Biotechnol., 3, 159-162 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.99.36

Cloned(Commentary)

Cloned (Comment) Organism
gene cypD, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Streptomyces coelicolor

Protein Variants

Protein Variants Comment Organism
additional information the generation of four cypemycin variants with modified AviCys moiety by site direct mutagenesis of the precursor peptide CypA Streptomyces coelicolor

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
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 C3.19,S21-cyclocypemycin(1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide + CO2 + H2S + reduced acceptor
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 ?
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
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 ?

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
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Streptomyces coelicolor M1414
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration Streptomyces coelicolor

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
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 Streptomyces coelicolor C3.19,S21-cyclocypemycin(1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide + CO2 + H2S + reduced acceptor
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 ?
cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys + acceptor
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 Streptomyces coelicolor M1414 C3.19,S21-cyclocypemycin(1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide + CO2 + H2S + reduced acceptor
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 ?
additional information CypD substrate specificity is tested with a series of synthetic oligopeptides, overview. The N-terminal sequence of CypA is not required for CypD activity, and the C-terminal three residues serve as the minimal structural element for enzyme recognition. CypD tolerates various substrates with modified C-termini, allowing for the generation of four cypemycin variants with modified AviCys moiety by site direct mutagenesis of the precursor peptide CypA.Relaxed substrate specificity of CypD. The CypD-catalyzed oxidative decarboxylation of the C-terminal Cys, a key step in the formation of the cypemycin AviCys moiety. CypD catalyzes oxidative decarboxylation of the CypA Cys22. LC-HR-MS analysis of each reaction mixture with peptides STISLEC or STISLKC shows that neither of these two peptides is decarboxylated, suggesting that CypD does not accept charged residues at the penultimate C-terminal position. Although peptide STISIVC is decarboxylated, no decarboxylated product of peptide STISKVC and STISYVC are observed, suggesting neither charged residues nor large aromatic residues can be accepted by CypD. Peptides QGSTISLVC, STISLVC, ISLVC, SLVC, and LVC are decarboxylated by CypD, whereas decarboxylation of peptide VC is not observed. The C-terminal three residues of CypA seem to serve as the minimal structural element for CypD recognition. Peptide STISLVS in which the C-terminal Cys is changed to Ser, is not decarboxylated by CypD, thus CypD is only able to act on Cys. Peptides STISLAC, STISLCC, and STISLIC are decarboyxlated, while peptide STISLYC is not decarboxylated by CypD, suggesting that the enzyme tolerates structural variation at the penultimate position to some extend, but does not accept large aromatic residue at this position. Although peptide STIALVC is decarboxylated, no decarboxylation is found for peptide STITLVC and STILLVC Streptomyces coelicolor ?
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additional information CypD substrate specificity is tested with a series of synthetic oligopeptides, overview. The N-terminal sequence of CypA is not required for CypD activity, and the C-terminal three residues serve as the minimal structural element for enzyme recognition. CypD tolerates various substrates with modified C-termini, allowing for the generation of four cypemycin variants with modified AviCys moiety by site direct mutagenesis of the precursor peptide CypA.Relaxed substrate specificity of CypD. The CypD-catalyzed oxidative decarboxylation of the C-terminal Cys, a key step in the formation of the cypemycin AviCys moiety. CypD catalyzes oxidative decarboxylation of the CypA Cys22. LC-HR-MS analysis of each reaction mixture with peptides STISLEC or STISLKC shows that neither of these two peptides is decarboxylated, suggesting that CypD does not accept charged residues at the penultimate C-terminal position. Although peptide STISIVC is decarboxylated, no decarboxylated product of peptide STISKVC and STISYVC are observed, suggesting neither charged residues nor large aromatic residues can be accepted by CypD. Peptides QGSTISLVC, STISLVC, ISLVC, SLVC, and LVC are decarboxylated by CypD, whereas decarboxylation of peptide VC is not observed. The C-terminal three residues of CypA seem to serve as the minimal structural element for CypD recognition. Peptide STISLVS in which the C-terminal Cys is changed to Ser, is not decarboxylated by CypD, thus CypD is only able to act on Cys. Peptides STISLAC, STISLCC, and STISLIC are decarboyxlated, while peptide STISLYC is not decarboxylated by CypD, suggesting that the enzyme tolerates structural variation at the penultimate position to some extend, but does not accept large aromatic residue at this position. Although peptide STIALVC is decarboxylated, no decarboxylation is found for peptide STITLVC and STILLVC Streptomyces coelicolor M1414 ?
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Synonyms

Synonyms Comment Organism
CYPD
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 Streptomyces coelicolor
cypemycin decarboxylase
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 Streptomyces coelicolor

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
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 assay at Streptomyces coelicolor

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
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 assay at Streptomyces coelicolor

Cofactor

Cofactor Comment Organism Structure
FAD dependent on Streptomyces coelicolor

General Information

General Information Comment Organism
additional information structure-function analysis, LC-HR-MS analysis, overview Streptomyces coelicolor