Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Kolli, N.; Garman, S.C.
    Proteolytic activation of human cathepsin A (2014), J. Biol. Chem., 289, 11592-11600.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.16.5 expressed as a flagged tagged fusion protein in Tn5 insect cells Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.16.5 crystal structure of mature cathepsin A is determined to 2.8 A resolution Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.4.16.5 R262A/R292A double mutant also undergoes processing to form large and small subunits, suggesting alternative avenues for the maturation of cathepsin A Homo sapiens
3.4.16.5 S150A/R284A/R298A triple mutant S150A/R284A/R298A also undergoes cleavage into large and small subunits, comparable with the wildtype cathepsin A, suggesting that these sites are not mandatory for the activation of cathepsin A Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.16.5 0.04
-
CBZ-Phe-Leu recombinant protein, pH 4.5, 27°C Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.16.5 51100
-
MALDI-TOF, mature protein. Enzymatic activity increases with maturation of Cathepsin A to the 51.1 kDa form Homo sapiens
3.4.16.5 54400
-
MALDI-TOF, zymogen protein Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.4.16.5 Homo sapiens P10619
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.16.5 proteolytic modification the activation of precursor cathepsin A is achieved by proteolytic removal of a larger 3.3-kDa peptide that includes the blocking peptide, bypassing the requirement for conformational changes Homo sapiens

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.16.5 using affinity and ion-exchange chromatography Homo sapiens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.16.5 additional information
-
enzymatic activity increases with maturation of cathepsin A to the 51.1 kDa form Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.16.5 CBZ-Phe-Leu + H2O
-
Homo sapiens N-benzyloxycarbonyl-L-Phe + L-leucine
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.16.5 CatA
-
Homo sapiens
3.4.16.5 cathepsin A
-
Homo sapiens
3.4.16.5 CTSA
-
Homo sapiens
3.4.16.5 HPP
-
Homo sapiens
3.4.16.5 PpcA
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.16.5 27
-
assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.16.5 12.1
-
CBZ-Phe-Leu recombinant protein, pH 4.5, 27°C Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.16.5 4.5
-
assay at Homo sapiens