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]

Cofactor

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Cofactor on EC 1.3.99.36 - cypemycin cysteine dehydrogenase (decarboxylating)

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

FAD

2 entries

additional information

Streptomyces coelicolor

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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

763030

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FAD

Streptomyces coelicolor

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dependent on

763314, 763536, 763750

FAD

Streptomyces coelicolor

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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

763030