3.4.13.21: dipeptidase E

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For detailed information about dipeptidase E, go to the full flat file.

Reaction

dipeptidase E catalyses the hydrolysis of dipeptides Asp-/-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides =

Synonyms

alpha-aspartyl dipeptidase, Asp-specific dipeptidase, aspartyl dipeptidase, dipeptidase E, PepE, PepE gene product, Salmonella typhimurium, peptidase E

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.13 Dipeptidases

                3.4.13.21 dipeptidase E

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Results	in table
2909	AA Sequence
1	CAS Registry Number
5	Cloned(Commentary)
3	Crystallization (Commentary)
6	Inhibitors
3	KM Value [mM]
1	Metals/Ions
4	Molecular Weight [Da]
26	Organism
6	PDB ID
12	pH Optimum
1	pH Range
6	Protein Variants
5	Purification (Commentary)
1	Reaction
1	Reaction Type
26	Reference
3	Specific Activity [micromol/min/mg]
40	Substrates and Products (Substrate)
1	Subunits
24	Synonyms
9	Temperature Optimum [°C]
1	Temperature Stability [°C]
3	Turnover Number [1/s]

Crystallization

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of the Enzyme Summary Page.

Crystallization on EC 3.4.13.21 - dipeptidase E

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Salmonella enterica subsp. enterica serovar Typhimurium

-

137205

aspartate-bound structure at 1.83 A resolution. The enzyme forms a dimer, and the active site is located at the dimer interface. The stringent aspartate specificity of the enzyme is due to electrostatics and molecular complementarity in the active site

Salmonella enterica subsp. enterica serovar Typhimurium

P36936

753575

crystal structure at 1.2 A resolution

Salmonella enterica subsp. enterica serovar Typhimurium

-

137202