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Information on EC 1.3.99.36 - cypemycin cysteine dehydrogenase (decarboxylating)
for references in articles please use BRENDA:EC1.3.99.36
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EC Tree 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)
IUBMB Comments
Cypemycin, isolated from the bacterium Streptomyces sp. OH-4156, is a peptide antibiotic, member of the linaridins, a class of posttranslationally modified ribosomally synthesized peptides. The enzyme decarboxylates and reduces the C-terminal L-cysteine residue, producing a reactive ethenethiol group that reacts with a dethiolated cysteine upstream to form an aminovinyl-methyl-cysteine loop that is important for the antibiotic activity of the mature peptide.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
cypemycin decarboxylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYPD
cypemycin decarboxylase
cypemycin dehydratase.
CYPD
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cypemycin decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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SYSTEMATIC NAME
IUBMB Comments
cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys:acceptor oxidoreductase (decarboxylating, cyclizing)
Cypemycin, isolated from the bacterium Streptomyces sp. OH-4156, is a peptide antibiotic, member of the linaridins, a class of posttranslationally modified ribosomally synthesized peptides. The enzyme decarboxylates and reduces the C-terminal L-cysteine residue, producing a reactive ethenethiol group that reacts with a dethiolated cysteine upstream to form an aminovinyl-methyl-cysteine loop that is important for the antibiotic activity of the mature peptide.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
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
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
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Substrates: -
Products: -
Products: -
?
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
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Substrates: -
Products: -
Products: -
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additional information
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Substrates: 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
Products: -
Products: -
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additional information
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Substrates: 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
Products: -
Products: -
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additional information
?
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Streptomyces coelicolor M1414
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Substrates: 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
Products: -
Products: -
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additional information
?
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Streptomyces coelicolor M1414
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Substrates: 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
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
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
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Substrates: -
Products: -
Products: -
?
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
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Substrates: -
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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S-[(Z)-2-aminovinyl]-D-cysteine (AviCys) is a unique structural motif found in several classes of RiPPs, including lanthipeptides (e.g. epidermin), lipolanthines (e.g., microvionine), polythioamides (e.g. thioviridamide), and linaridins (e.g. cypemycin). Enzyme structure-function analysis, overview
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FAD
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dependent on. Binding structure analysis, overview. Each monomer associates with a flavin adenine dinucleotide (FAD) cofactor. The adenine ring of FAD sits in the central cavity of a CypD trimer and forms no direct interactions with any monomers. The rest of the molecule is embedded only at the interface of two monomers, among which one predominantly interacts with FAD. This particular monomer mainly interacts with the phosphoribityl moiety of FAD via the residues in the N-termini of its three helices, namely, Ser18 in a1, Thr45 and Ala47 in a2, and Thr96 in alpha5. Specifically, Ser18, Leu97, and Thr128 form polar interactions with the isoalloxazine ring, whereas Thr45, Thr96, and Thr99 are hydrogen bonded to the oxygen atoms of phosphoribitol backbone. Meanwhile, Thr47, Arg107, and Asp109 interact with the adenosine monophosphate group: the first two residues form hydrogen bonds with the phosphate, whereas Asp109 forms similar interactions with two hydroxyl groups on the ribose ring. The second monomer forms much less interactions with FAD. Phe'51 has a weak hydrophobic contact with the isoalloxazine ring. Ala'108 and Arg'107 are hydrogen bonded to hydroxyls on the ribitol chain and ribose ring, respectively. Three water molecules are bound to the phosphoribityl backbone, of which one (Wat1) also interacts with N1 and O2 of the isoalloxazine ring. The crystal structure of the cypemycin decarboxylase CypD shows that CypD is structurally highly similar to lanthipeptide decarboxylases despite the absence of sequence similarities between them
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
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CypD possesses a structural fold highly similar to two structurally characterized LanDs (EpiD in epidermin biosynthesis and MrsD in mersacidin biosynthesis). Similar to CypD, the substrate binding clamps are also not observed in the crystal structures of EpiD and MrsD when the peptide substrate is absent. But because CypD shares no detectable sequence similarity with these two LanDs, this finding reveals a convergent evolution in AviCys biosynthesis
evolution
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flavin-dependent Cys decarboxylases are highly divergent among different RiPP classes. Cys decarboxylases from four RiPP classes have evolved independently and form two major clusters. Convergent evolution of AviCys biosynthesis, all the flavin-dependent Cys decarboxylases likely have a similar Rossmann fold despite their sequence divergences. Evolution of Cys decarboxylases involved in AviCys biosynthesis, overview
evolution
Streptomyces coelicolor M1414
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flavin-dependent Cys decarboxylases are highly divergent among different RiPP classes. Cys decarboxylases from four RiPP classes have evolved independently and form two major clusters. Convergent evolution of AviCys biosynthesis, all the flavin-dependent Cys decarboxylases likely have a similar Rossmann fold despite their sequence divergences. Evolution of Cys decarboxylases involved in AviCys biosynthesis, overview
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evolution
Streptomyces coelicolor M1414
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CypD possesses a structural fold highly similar to two structurally characterized LanDs (EpiD in epidermin biosynthesis and MrsD in mersacidin biosynthesis). Similar to CypD, the substrate binding clamps are also not observed in the crystal structures of EpiD and MrsD when the peptide substrate is absent. But because CypD shares no detectable sequence similarity with these two LanDs, this finding reveals a convergent evolution in AviCys biosynthesis
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physiological function
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linaridins are a small but growing class of natural products belonging to the ribosomally synthesized and posttranslationally modified peptide (RiPP) superfamily. The class A linaridins, exemplified by cypemycin, possess an unusual S-[(Z)-2-aminovinyl]-D-cysteine (AviCys) residue. Formation of the AviCys in cypemycin requires an oxidative decarboxylation of the precursor peptide C-terminal Cys, and this reaction is catalyzed by a flavin-dependent decarboxylase CypD. Analysis of the molecular recognition processes of CypD by a combination of computational and biochemical analysis, overview
physiological function
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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
physiological function
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S-[(Z)-2-aminovinyl]-D-cysteine (AviCys) is a unique motif found in several classes of ribosomally synthesized and posttranslationally modified peptides (RiPPs). Biosynthesis of AviCys requires flavin-dependent Cys decarboxylases, which are highly divergent among different RiPP classes
physiological function
Streptomyces coelicolor M1414
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S-[(Z)-2-aminovinyl]-D-cysteine (AviCys) is a unique motif found in several classes of ribosomally synthesized and posttranslationally modified peptides (RiPPs). Biosynthesis of AviCys requires flavin-dependent Cys decarboxylases, which are highly divergent among different RiPP classes
-
physiological function
Streptomyces coelicolor M1414
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linaridins are a small but growing class of natural products belonging to the ribosomally synthesized and posttranslationally modified peptide (RiPP) superfamily. The class A linaridins, exemplified by cypemycin, possess an unusual S-[(Z)-2-aminovinyl]-D-cysteine (AviCys) residue. Formation of the AviCys in cypemycin requires an oxidative decarboxylation of the precursor peptide C-terminal Cys, and this reaction is catalyzed by a flavin-dependent decarboxylase CypD. Analysis of the molecular recognition processes of CypD by a combination of computational and biochemical analysis, overview
-
physiological function
Streptomyces coelicolor M1414
-
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
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additional information
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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
additional information
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movements of the substrate-binding clamp of cypemycin decarboxylase CypD, mechanism, substrate-induced secondary structure change in CypD, overview. The substrate binding clamp of CypD undergoes dramatic fluctuation. Structure and motion of the missing region by performing 3 × 300 ns unbiased molecular dynamics (MD) analysis, and principle component analysis (PCA) is utilized to analyze the protein backbone motion in MD trajectory. The substrate binding clamp of CypD undergoes dramatic fluctuation, mediating both the substrate entrance into and product release from the catalytic pocket. Extensive molecular dynamic simulations and Fourier transform IR analyses indicate that binding of the substrate induces substantial structural change of the enzyme, converting the substrate-binding clamp from a random loop to a more ordered structure comprising two beta sheets and a beta turn. The salt bridge between Arg159 guanine and the Cys carboxylate of substrate plays an important role in mediating substrate binding, while hydrophobic interactions are also important in this process. Computational construction of a CypD-substrate complex and interaction analysis. The carboxyl group of substrate forms a salt bridge with the guanine moiety of Arg159 and also hydrogen bonds with the amide NH of Ala160 and Ser161. A hydrogen bond is also found between the Val158 C=O and the penultimate amide NH in the C-terminus. The substrate also interacts with several residues (e.g. Leu23, Trp26, Trp27, Val155, Val168) via hydrophobic interactions
additional information
-
structure-function analysis, LC-HR-MS analysis, overview
additional information
Streptomyces coelicolor M1414
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movements of the substrate-binding clamp of cypemycin decarboxylase CypD, mechanism, substrate-induced secondary structure change in CypD, overview. The substrate binding clamp of CypD undergoes dramatic fluctuation. Structure and motion of the missing region by performing 3 × 300 ns unbiased molecular dynamics (MD) analysis, and principle component analysis (PCA) is utilized to analyze the protein backbone motion in MD trajectory. The substrate binding clamp of CypD undergoes dramatic fluctuation, mediating both the substrate entrance into and product release from the catalytic pocket. Extensive molecular dynamic simulations and Fourier transform IR analyses indicate that binding of the substrate induces substantial structural change of the enzyme, converting the substrate-binding clamp from a random loop to a more ordered structure comprising two beta sheets and a beta turn. The salt bridge between Arg159 guanine and the Cys carboxylate of substrate plays an important role in mediating substrate binding, while hydrophobic interactions are also important in this process. Computational construction of a CypD-substrate complex and interaction analysis. The carboxyl group of substrate forms a salt bridge with the guanine moiety of Arg159 and also hydrogen bonds with the amide NH of Ala160 and Ser161. A hydrogen bond is also found between the Val158 C=O and the penultimate amide NH in the C-terminus. The substrate also interacts with several residues (e.g. Leu23, Trp26, Trp27, Val155, Val168) via hydrophobic interactions
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additional information
Streptomyces coelicolor M1414
-
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
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additional information
Streptomyces coelicolor M1414
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structure-function analysis, LC-HR-MS analysis, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
dodecamer
-
a CypD monomer consists of a single classic Rossmann-fold domain, which is composed of a central beta-sheet formed by six parallel strands (labeled beta1-beta6) enclosed by eight alpha helices (labeled alpha1-alpha8). Residues that participate in forming the trimer (trimer contacts) are found in a region spanning alpha5 and alpha6, and a region containing alpha7 and a long loop in the terminus of alpha7, whereas interactions between trimers (dimer contacts) are found mainly within alpha1, and a region spanning alpha2 and alpha3
dodecamer
-
each monomer consists of a classic Rossmann-fold domain. This domain is constructed by a central beta sheet consisting of six parallel strands, which are enclosed by eight alpha helices. A fragment spanning Asn156-Ala166 is not observed in the CypD structure, which is likely responsible in substrate binding
dodecamer
Streptomyces coelicolor M1414
-
a CypD monomer consists of a single classic Rossmann-fold domain, which is composed of a central beta-sheet formed by six parallel strands (labeled beta1-beta6) enclosed by eight alpha helices (labeled alpha1-alpha8). Residues that participate in forming the trimer (trimer contacts) are found in a region spanning alpha5 and alpha6, and a region containing alpha7 and a long loop in the terminus of alpha7, whereas interactions between trimers (dimer contacts) are found mainly within alpha1, and a region spanning alpha2 and alpha3
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dodecamer
Streptomyces coelicolor M1414
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each monomer consists of a classic Rossmann-fold domain. This domain is constructed by a central beta sheet consisting of six parallel strands, which are enclosed by eight alpha helices. A fragment spanning Asn156-Ala166 is not observed in the CypD structure, which is likely responsible in substrate binding
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, X-ray diffraction structure determination and analysis at 2.6 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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the generation of four cypemycin variants with modified AviCys moiety by site direct mutagenesis of the precursor peptide CypA
additional information
Streptomyces coelicolor M1414
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the generation of four cypemycin variants with modified AviCys moiety by site direct mutagenesis of the precursor peptide CypA
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
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recombinant SeMet-substituted CypD from Escherichia coli strain BL21(DE3)
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cypD, phylogenetic tree, recombinant expression of SeMet-substituted CypD in Escherichia coli strain BL21(DE3)
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gene cypD, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Claesen, J.; Bibb, M.
Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides
Proc. Natl. Acad. Sci. USA
107
16297-16302
2010
Streptomyces sp., Streptomyces sp. OH-4156
brenda
Mo, T.; Yuan, H.; Wang, F.; Ma, S.; Wang, J.; Li, T.; Liu, G.; Yu, S.; Tan, X.; Ding, W.; Zhang, Q.
Convergent evolution of the Cys decarboxylases involved in aminovinyl-cysteine (AviCys) biosynthesis
FEBS Lett.
593
573-580
2019
Streptomyces coelicolor, Streptomyces coelicolor M1414
brenda
Liu, L.; Chan, S.; Mo, T.; Ding, W.; Yu, S.; Zhang, Q.; Yuan, S.
Movements of the substrate-binding clamp of cypemycin decarboxylase CypD
J. Chem. Inf. Model.
59
2924-2929
2019
Streptomyces coelicolor, Streptomyces coelicolor M1414
brenda
Ding, W.; Yuan, N.; Mandalapu, D.; Mo, T.; Dong, S.; Zhang, Q.
Cypemycin decarboxylase CypD is not responsible for aminovinyl-cysteine (AviCys) ring formation
Org. Lett.
20
7670-7673
2018
Streptomyces coelicolor, Streptomyces coelicolor M1414
brenda
Ding, W.; Mo, T.; Mandalapu, D.; Zhang, Q.
Substrate specificity of the cypemycin decarboxylase CypD
Synth. Syst. Biotechnol.
3
159-162
2018
Streptomyces coelicolor, Streptomyces coelicolor M1414
brenda
EXTERNAL LINKS (specific for EC-Number 1.3.99.36)
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Release 2023.1 (January 2023)
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