3.4.24.89: Pro-Pro endopeptidase

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For detailed information about Pro-Pro endopeptidase, go to the full flat file.

Reaction

The enzyme catalyses the hydrolytic cleavage of peptide bonds between two proline residues =

Synonyms

CD2830, CD630_28300, PPEP-1, PPEP-2, Pro-Pro endopeptidase, Pro-Pro endopeptidase 1, proline-proline endopeptidase-1, Zmp1

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.89 Pro-Pro endopeptidase

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Results	in table
3	AA Sequence
4	Cloned(Commentary)
3	Crystallization (Commentary)
1	Expression
6	General Information
1	Inhibitors
6	kcat/KM [mM/s]
7	KM Value [mM]
5	Localization
6	Metals/Ions
19	Natural Substrates/ Products (Substrates)
33	Organism
39	PDB ID
25	Protein Variants
2	Purification (Commentary)
2	Reaction
1	Reaction Type
13	Reference
2	Source Tissue
47	Substrates and Products (Substrate)
6	Subunits
21	Synonyms
7	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.24.89 - Pro-Pro endopeptidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Clostridioides difficile

Q183R7

754181

crystal structures of Zmp1 in its unbound and peptide-bound forms. The structure analysis reveals a fold similar to Bacillus anthracis lethal factor. The structure consists of an upper N-terminal domain and a lower helical C-terminal domain with respect to the active-site helix aalpha4, which harbors two of the three zinc-binding residues His142 and His146 and the catalytic base Glu143 in the typical metalloprotease motif (H142E143TAH146)

Clostridioides difficile

Q183R7

735291

using 2.2 M (NH4)2SO4, 0.2 M CdSO4, 0.01 M ZnCl2 (pH 9.0)

Paenibacillus alvei

K4ZRC1

754163