3.4.23.25: saccharopepsin

This is an abbreviated version!
For detailed information about saccharopepsin, go to the full flat file.

Reaction

Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-/-Val-Tyr bond in a synthetic substrate. Does not act on esters of Tyr or Arg =

Synonyms

Acid protease, Aspartate protease, Aspartic proteinase, Aspartic proteinase yscA, EC 3.4.23.6, EC 3.4.23.8, EC 3.4.4.17, Pep4, PEP4 gene product, Pep4p, Pep4p vacuolar proteinase, pepsin-like aspartic proteinase, PRA, preproPrA, proPrA, Protease A, Proteinase A, proteinase A precursor, Proteinase yscA, Proteinase, yeast A, proteinase-A, pseudo-proteinase A, Saccharomyces aspartic proteinase, Saccharomyces cerevisiae aspartic proteinase A, saccharopepsin, vacuolar aspartic proteinase, yeast aspartic proteinase A, Yeast endopeptidase A, yeast proteinase, Yeast proteinase A

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.23 Aspartic endopeptidases

                3.4.23.25 saccharopepsin

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Results	in table
2	Activating Compound
18	AA Sequence
9	Application
1	CAS Registry Number
5	Cloned(Commentary)
6	Crystallization (Commentary)
3	Expression
2	General Information
3	General Stability
1	IC50 Value
50	Inhibitors
47	Ki Value [mM]
39	KM Value [mM]
21	Localization
18	Molecular Weight [Da]
15	Natural Substrates/ Products (Substrates)
76	Organism
12	PDB ID
14	pH Optimum
4	pH Range
4	pH Stability
9	Posttranslational Modification
5	Protein Variants
13	Purification (Commentary)
3	Reaction
1	Reaction Type
43	Reference
1	Source Tissue
4	Specific Activity [micromol/min/mg]
2	Storage Stability
115	Substrates and Products (Substrate)
15	Subunits
75	Synonyms
2	Temperature Optimum [°C]
3	Temperature Stability [°C]
40	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.23.25 - saccharopepsin

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Saccharomyces cerevisiae

-

652130

bound to inhibitor protein IA3, vapor diffusion, space group P6(2)22, unit cell dimensions a = b = 192.66 A, c = 52.09 A

Saccharomyces cerevisiae

-

653309

crystallized with and without non-hydrolyzable transition-state analogue inhibitors

Saccharomyces cerevisiae

-

30707

in complex with natural aspartic proteinase in hibitor IA3, space group P6(2)22, with unit-cell parameters a : b : 192.1 A, c : 59.80 A, native saccharopepsin crystals belongs to the orthorhombic space group I2(1)2(1)2(1) with unit-cell parameters a : 101.4 A, b 0 128.7 A, c : 155.4 A, in complex with CP81,282 and PD130,327 trigonal space group P3(2)21, with unit-cell parameters a 0 b : 87.4 A, c : 110.2 A

Saccharomyces cerevisiae

-

649129

structures of the native enzyme solved by molecular replacement in monoclinic and trygonal crystal forms, trigonal space group P3(2)21, cell dimensions a = b = 84.6 A, c = 108.7 A, monoclinic space group P2(1), cell dimensions a = 82.97 A, b = 49.08 A, c = 94.69 A

Saccharomyces cerevisiae

P07267

649600

vapour diffusion, space group P3(2)21, in complex with inhibitor CP-81,198 unit cell dimensions a : b : 86.8 A, c : 110.2 A, in complex with inhibitor CP-108,420 unit cell dimensions a : b : 86.9 A, c : 110.2 A, in complex with inhibitor CP-72,647 unit cell dimensions a : b : 86.4 A, c : 109.9 A, in complex with inhibitor PD-129,541 unit cell dimensions a : b : 87.3 A, c : 110.7 A, in complex with inhibitor PD-133,450 unit cell dimensions a : b : 86.9 A, c : 110.2 A

Saccharomyces cerevisiae

-

652836