1.3.99.36: cypemycin cysteine dehydrogenase (decarboxylating)

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For detailed information about cypemycin cysteine dehydrogenase (decarboxylating), go to the full flat file.

Reaction

Synonyms

CYPD, cypemycin decarboxylase, cypemycin dehydratase.

ECTree

     1 Oxidoreductases

         1.3 Acting on the CH-CH group of donors

             1.3.99 With unknown physiological acceptors

                1.3.99.36 cypemycin cysteine dehydrogenase (decarboxylating)

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Results	in table
3	AA Sequence
2	Cloned(Commentary)
5	Cofactor
1	Crystallization (Commentary)
16	General Information
8	Natural Substrates/ Products (Substrates)
23	Organism
1	PDB ID
1	pH Optimum
2	Protein Variants
2	Purification (Commentary)
1	Reaction
10	Reference
12	Substrates and Products (Substrate)
4	Subunits
16	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]

Substrates Products

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Substrates Products on EC 1.3.99.36 - cypemycin cysteine dehydrogenase (decarboxylating)

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SUBSTRATE

PRODUCT                       

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

Reversibility
r=reversible
ir=irreversible
?=not specified

cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys + acceptor

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

2 entries

additional information

?

-

4 entries

cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys + acceptor

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

Streptomyces coelicolor

-

-

763030, 763314, 763536, 763750

-

-

?

cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys + acceptor

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

Streptomyces coelicolor M1414

-

-

763030, 763314, 763536, 763750

-

-

?

additional information

?

-

Streptomyces coelicolor

-

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

763750

-

-

-

additional information

?

-

Streptomyces coelicolor

-

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

763536

-

-

-

additional information

?

-

Streptomyces coelicolor M1414

-

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

763536

-

-

-

additional information

?

-

Streptomyces coelicolor M1414

-

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

763750

-

-

-