3.4.21.57: Leucyl endopeptidase

This is an abbreviated version, for detailed information about Leucyl endopeptidase, go to the full flat file.

Reaction

Hydrolysis of proteins. Preferential cleavage: Leu-/- in small molecule substrates =

Synonyms

Leu-proteinase, Leucine endopeptidase, Leucine-specific serine proteinase, Plant Leu-proteinase, Proteinase, leucine-specific, Proteinase, spinach serine (leucine specific), Spinach leucine-specific serine proteinase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.57 Leucyl endopeptidase

Reference

Reference on EC 3.4.21.57 - Leucyl endopeptidase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Aducci, P.; Ascenzi, P.; Pierini, M.; Ballio, A.
Purification and characterization of Leu-proteinase, the leucine specific serine proteinase from spinach (Spinacia oleracea L.) leaves
Plant Physiol.
81
812-816
1986
Spinacia oleracea
Manually annotated by BRENDA team
Aducci, P.; Ascenzi, P.; Ballio, A.
Esterolytic properties of leucine-proteinase, the leucine-specific serine proteinase from spinach (Spinacia oleracea L.) leaves. A steady-state and pre-steady-state study
Plant Physiol.
82
591-593
1986
Spinacia oleracea
Manually annotated by BRENDA team
Ascenzi, P.; Amiconi, G.; Ballio, A.; Bolognesi, M.; Menegatti, E.; Schnebli, H.P.; Aducci, P.
Binding of the recombinant proteinase inhibitor eglin c, of the soybean Bowman-Birk proteinase inhibitor and of its chymotrypsin and trypsin inhibiting fragments to Leu-proteinase, the leucine specific serine proteinase from spinach (Spinacia oleracea L.) leaves: thermodynamic study
J. Enzyme Inhib.
4
283-288
1991
Spinacia oleracea
Manually annotated by BRENDA team
Kim, J.I.; Lee, S.M.; Jung, H.J.
Characterization of calcium-activated bifunctional peptidase of the psychrotrophic Bacillus cereus
J. Microbiol.
43
237-243
2005
Bacillus cereus
Manually annotated by BRENDA team