3.4.24.B24: L-alanine-D-glutamate endopeptidase

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For detailed information about L-alanine-D-glutamate endopeptidase, go to the full flat file.

Reaction

endohydrolysis of the linkage of L-alanine-D-glutamic acid in the stem of a peptidoglycan =

Synonyms

CwlK, L,D-endopeptidase, L-alanoyl-D-glutamate endopeptidase, L-alanoyl-D-glutamate peptidase, Peptidoglycan hydrolase, peptidoglycan L-alanyl-D-glutamate endopeptidase cwIK, Ply500, TagX, YcdD

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.B24 L-alanine-D-glutamate endopeptidase

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Results	in table
2	AA Sequence
1	Application
3	Cloned(Commentary)
1	Crystallization (Commentary)
1	General Information
3	Localization
1	Metals/Ions
2	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
3	Organism
1	pH Optimum
1	Posttranslational Modification
1	Protein Variants
2	Purification (Commentary)
1	Reaction
2	Reaction Type
3	Reference
3	Substrates and Products (Substrate)
1	Subunits
12	Synonyms
1	Temperature Optimum [°C]

Crystallization

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Crystallization on EC 3.4.24.B24 - L-alanine-D-glutamate endopeptidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

the crystal structure of the enzymatically active domain of Ply500 is solved at 1.8 A resolution

Listeria phage A500

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