3.4.21.83: Oligopeptidase B

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

Reaction

Hydrolysis of -Arg-/-, -Lys-/- bonds in oligopeptides, even when P1' residue is proline =

Synonyms

La_OpB, oligopeptidase B, oligopeptidase B-like, oligopeptidase B2, OP-Tb, OPB, OPB2, OPBTc, Opd B, OpdB, Protease II, Proteinase, Escherichia coli alkaline, II, PSP, Spro_3467, Tb-OP, Tc 120, Tc-OP, trypsin-like protease

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.83 Oligopeptidase B

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Results	in table
11	Activating Compound
5059	AA Sequence
3	Application
1	CAS Registry Number
24	Cloned(Commentary)
5	Crystallization (Commentary)
19	General Information
4	General Stability
1	IC50 Value
99	Inhibitors
86	kcat/KM [mM/s]
30	Ki Value [mM]
344	KM Value [mM]
3	Localization
5	Metals/Ions
20	Molecular Weight [Da]
3	Natural Substrates/ Products (Substrates)
3	Organic Solvent Stability
55	Organism
9	PDB ID
17	pH Optimum
6	pH Range
3	pH Stability
2	pI Value
2	Posttranslational Modification
69	Protein Variants
16	Purification (Commentary)
1	Reaction
1	Reaction Type
51	Reference
7	Source Tissue
62	Specific Activity [micromol/min/mg]
4	Storage Stability
384	Substrates and Products (Substrate)
15	Subunits
64	Synonyms
17	Temperature Optimum [°C]
4	Temperature Range [°C]
14	Temperature Stability [°C]
332	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.21.83 - Oligopeptidase B

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

using the hanging-drop vapour-diffusion technique in 7%(w/v) polyethylene glycol 6000, 1 M LiCl, 0.1 M bis-tris propane pH 7.5. Diffraction data to 2.7 A resolution are collected using synchrotron radiation. The crystals belong to space group P3121 or P3221, with unit-cell parameters a = b = 124.5, c = 249.9 A. A complete data set to 2.7 A is collected using synchrotron radiation

Leishmania amazonensis

A7XAB0

683954

in complex with the inhibitor antipain and as mercury derivative, to 1.65 and 2.0 A resolution, respectively. OPB comprises two domains, a catalytic and a propeller domain, linked together by a hinge region. Residue E621 plays a critical role in the S1 binding pocket and, along with F603, is largely responsible for the enzyme substrate specificity in P1. In the S2 binding pocket, Y499 is important for substrate stability. Residue E623 forms an inter-domain hydrogen bond

Leishmania major

Q4QHU7

717812

crystal structure solved at 2.7 A resolution

Trypanosoma brucei

Q382P7

683194

using the hanging-drop vapour-diffusion technique in 7% (w/v) polyethylene glycol 6000, 1 M LiCl, 0.1 M bis-tris propane pH 7.5. Diffraction data to 2.7 A resolution are collected using synchrotron radiation. The crystals belong to space group P3121 or P3221, with unit-cell parameters a = b = 124.5, c = 249.9 A. A complete data set to 2.7 A is collected using synchrotron radiation

Trypanosoma brucei

-

683025

ligand-free open state and inhibitor-bound closed state crystal structures, to 2.4 and 2.85 A resolution, respectively. Peptides over 30 residues cannot fit the enzyme cavity, preventing the complete domain closure required for a key propeller Asp/Glu to fix the catalytic His and Arg in the catalytically competent conformation. This size exclusion mechanism protects larger peptides and proteins from degradation

Trypanosoma brucei brucei

O76728

732756