From Wikipedia, the free encyclopedia
Xaa-Arg dipeptidase
Identifiers
EC no. 3.4.13.4
CAS no. 37288-72-5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Xaa-Arg dipeptidase ( EC 3.4.13.4, aminoacyl-lysine dipeptidase, N2-(4-amino-butyryl)-L-lysine hydrolase, X-Arg dipeptidase) is an enzyme. [1] This enzyme catalyses the following chemical reaction

Preferential hydrolysis of Xaa!Arg, Xaa!Lys or Xaa! ornithine dipeptides

This enzyme is widely distributed in mammals.

References

  1. ^ Kumon A, Matsuoka Y, Kakimoto Y, Nakajima T, Sano I (March 1970). "A peptidase that hydrolyzes Na-(gamma-aminobutyryl)lysine". Biochimica et Biophysica Acta (BBA) - Protein Structure. 200 (3): 466–74. doi: 10.1016/0005-2795(70)90103-0. PMID  5436646.
From Wikipedia, the free encyclopedia
Xaa-Arg dipeptidase
Identifiers
EC no. 3.4.13.4
CAS no. 37288-72-5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Xaa-Arg dipeptidase ( EC 3.4.13.4, aminoacyl-lysine dipeptidase, N2-(4-amino-butyryl)-L-lysine hydrolase, X-Arg dipeptidase) is an enzyme. [1] This enzyme catalyses the following chemical reaction

Preferential hydrolysis of Xaa!Arg, Xaa!Lys or Xaa! ornithine dipeptides

This enzyme is widely distributed in mammals.

References

  1. ^ Kumon A, Matsuoka Y, Kakimoto Y, Nakajima T, Sano I (March 1970). "A peptidase that hydrolyzes Na-(gamma-aminobutyryl)lysine". Biochimica et Biophysica Acta (BBA) - Protein Structure. 200 (3): 466–74. doi: 10.1016/0005-2795(70)90103-0. PMID  5436646.

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