3.4.23.40: Phytepsin

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

Reaction

Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-/-Asp- and -Asp-/-Asp- bonds in 2S albumin from plant seeds =

Synonyms

Acid protease, Ap1, Aspartic proteinase, Aspartyl endoproteinase, Barley grain aspartic proteinase, Carboxyl proteinase, CardA, cardB, Cardosin, cardosin A, cardosin B, Cynarase, cynarase A, cynarase B, cynarase C, Edestinase, HvAP, Nepenthesin, Oryzasin, PCB, procardosin B

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.23 Aspartic endopeptidases

                3.4.23.40 Phytepsin

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Results	in table
63	AA Sequence
3	Application
1	CAS Registry Number
4	Cloned(Commentary)
2	Crystallization (Commentary)
2	Expression
2	General Information
15	Inhibitors
7	kcat/KM [mM/s]
4	Ki Value [mM]
10	KM Value [mM]
2	Localization
48	Molecular Weight [Da]
19	Natural Substrates/ Products (Substrates)
43	Organism
3	PDB ID
31	pH Optimum
6	pH Range
1	pH Stability
4	pI Value
8	Posttranslational Modification
1	Protein Variants
5	Purification (Commentary)
1	Reaction
1	Reaction Type
43	Reference
39	Source Tissue
2	Specific Activity [micromol/min/mg]
2	Storage Stability
68	Substrates and Products (Substrate)
16	Subunits
24	Synonyms
5	Temperature Optimum [°C]
1	Temperature Range [°C]
6	Temperature Stability [°C]
9	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.23.40 - Phytepsin

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

to 1.72 A resoultion. Structure includes two molecules, built up by two glycosylated peptide chains of 31 and 15 kDa. The glycosyl content is described by 19 sugar rings attached to residues Asn67 and Asn257 localized on the molecular surface away from the conserved active site. A hydrogen bond between Gln126 and Manbeta4 renders the monosaccharide oxygen O2 sterically inaccessible to accept a xylosyl residue, explaining a hitherto unknown type of plant glycan. The Arg-Gly-Asp sequence, involved in recognition of a putative cardosin A receptor, is found in a loop between two beta-strands on the molecular surface opposite the active site cleft

Cynara cardunculus

Q9XFX3

734130

analysis of solvent structure in crystals, comparison of aspartic proteases, zymogen form

Hordeum vulgare

-

649256