3.4.23.5: cathepsin D
This is an abbreviated version!
For detailed information about cathepsin D, go to the full flat file.
Word Map on EC 3.4.23.5
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3.4.23.5
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lysosomal
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pepstatin
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estrogen
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metastasis
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alzheimer
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proteinases
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aspartyl
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node
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vacuole
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lymph
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renin
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pepsin
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endosomes
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progesterone
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hydrolases
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endocytic
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phagosomes
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amyloid
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beta-glucuronidase
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plasminogen
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mannose
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6-phosphate
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axillary
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autophagosomes
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saposins
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lysosomal-associated
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leupeptin
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plasmepsins
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beta-hexosaminidase
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missorting
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mannose-6-phosphate
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chymosin
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lysotracker
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lipofuscinosis
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lc3-ii
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autophagy-lysosomal
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rab7
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ceroid
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estrogen-regulated
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immunoradiometric
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medicine
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lc3
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lamp-1
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node-negative
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trans-golgi
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upa
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endocytosed
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node-positive
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c-erbb-2
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autolysosomes
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cation-independent
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molecular biology
- 3.4.23.5
- lysosomal
- pepstatin
- estrogen
- metastasis
- alzheimer
- proteinases
-
aspartyl
- node
- vacuole
- lymph
- renin
- pepsin
- endosomes
- progesterone
- hydrolases
-
endocytic
-
phagosomes
-
amyloid
- beta-glucuronidase
- plasminogen
- mannose
- 6-phosphate
-
axillary
-
autophagosomes
-
saposins
-
lysosomal-associated
- leupeptin
-
plasmepsins
- beta-hexosaminidase
-
missorting
- mannose-6-phosphate
- chymosin
-
lysotracker
- lipofuscinosis
-
lc3-ii
-
autophagy-lysosomal
- rab7
-
ceroid
-
estrogen-regulated
-
immunoradiometric
- medicine
- lc3
- lamp-1
-
node-negative
-
trans-golgi
- upa
-
endocytosed
-
node-positive
-
c-erbb-2
-
autolysosomes
-
cation-independent
- molecular biology
Reaction
Specificity similar to, but narrower than, that of pepsin A. Does not cleave the Gln4-His bond in B chain of insulin =
Synonyms
BmCatD, CAD 1, CAD 2, CAD 3, CapD, Cat D, CAT-D, CatD, Cath D, cath-D, cathD, cathepsin D, cathepsin D-like proteinase, cathepsin D1, cathepsin D2, CD1, CTSD, EC 3.4.4.23, matCTSD, PCD, Pep4p, preproCatD, pro-cathepsin, pro-cathepsin D, pro-CD, pro-CtsD, proCat, proCDrec, proCTSD, Proteinase A
ECTree
3.4.23.5 cathepsin DAdvanced search results
results (
results (Subunits
Subunits on EC 3.4.23.5 - cathepsin D
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
heterodimer
monomer
trimer
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1 * 27400, subunit A, + 1 * 24600, subunit B, + 1 * 13800, subunit C, SDS-PAGE
additional information
?
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two enzyme forms exist: a single 47000 Da polypeptide and a complex of 30000 Da subunit plus a 16500 Da subunit, SDS-PAGE
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x * 36412, mature cathepsin D, calculated from amino acid sequence
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x * 43106, pre-pro-cathepsin D, calculated from amino acid sequence
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x * 20000-60000, SDS-PAGE, epididymosomes possess many enzyme forms ranging from 20 to 60 kDa with the highest reactive intensity at the 26000 and 34000 Da bands
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x * 36000, mature cathepsin D, calculated from amino acid sequence
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two polypeptide chains: a 97-residue light chain and a 242-residue heavy chain, the MW of the heavy chain is 36779 Da, without carbohydrate, calculated from amino acid sequence
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one main band of 31000 Da and two minor bands of 15000 Da and 43000 Da, SDS-PAGE
dimer
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1 * 12000 + 1 * 34000, the enzyme also exists as a single chain enzyme form
additional information
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exist as precursor (53000-50000 Da),intermediate (48000-45000 Da) and mature (33000-30000 Da) isoforms, SDS-PAGE
additional information
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synthesized as single polypeptide chain that is proteolytically processed into mature CatD that exist as a two-chain form: an amino terminal light chain (14000 Da) and a carboxyl-terminal heavy chain (34000 Da), associated by hydrophobic interactions
