3.4.19.1: acylaminoacyl-peptidase

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

Reaction

cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide =

Synonyms

AAP, AARE, AARE/OPH, AAREP, AcpH, acyl aminoacyl peptidase, acyl peptide hydrolase, Acyl-peptide hydrolase, acyl-peptide releasing enzyme, acylamino acid-releasing enzyme, acylamino acid-releasing enzyme/oxidized protein hydrolase, acylamino-acid-releasing enzyme, acylaminoacyl peptidase, Acylaminoacyl-peptidase, acylpeptide hydrolase, acylpeptide hydrolase/esterase, alpha-N-acylpeptide hydrolase, ApAAP, apAPH, APEH, APEH-1, apeH-2, APEH-3, APEH-3Ss, APEHs, APE_1547.1, APH, APHdr, AtAARE, BmAPH, cAARE, DNF15S2 protein, N-acylaminoacyl-peptide hydrolase, N-acylpeptide hydrolase, N-formylmethionine (fMet) aminopeptidase, OP85, PhAAP, pi-APH, PM hydrolase, PMH, SpAAP, sso2141, SSO2693, ST0779, yuxL

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.19 Omega peptidases

                3.4.19.1 acylaminoacyl-peptidase

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Results	in table
1	Activating Compound
3067	AA Sequence
16	Application
1	CAS Registry Number
26	Cloned(Commentary)
13	Crystallization (Commentary)
420	Disease/ Diagnostics
5	Expression
50	General Information
10	General Stability
63	IC50 Value
180	Inhibitors
19	kcat/KM [mM/s]
9	Ki Value [mM]
96	KM Value [mM]
16	Localization
3	Metals/Ions
40	Molecular Weight [Da]
9	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
366	Organism
1	Pathway
48	PDB ID
35	pH Optimum
9	pH Range
5	pH Stability
1	pI Value
56	Protein Variants
36	Purification (Commentary)
2	Reaction
11	Reaction Type
118	Reference
1	Renatured (Commentary)
77	Source Tissue
48	Specific Activity [micromol/min/mg]
2	Storage Stability
342	Substrates and Products (Substrate)
50	Subunits
177	Synonyms
28	Temperature Optimum [°C]
6	Temperature Range [°C]
19	Temperature Stability [°C]
75	Turnover Number [1/s]

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

complete recovery of enzyme denatured with 8 M urea on dialysis or 50fold dilution. The enzyme loses its secondary structure at urea concentrations of 2 M and higher, whereas the tertiary structure is minimally perturbed below 4 M urea. Dialysis of the enzyme denatured with 1 M guanidine-HCl results in 15-20% recovery of enzyme activity. In 1 M guanidine HCl the enzyme loses both its secondary and tertiary structures and dissociates into monomers of 70000 Da. Both monomeric and dimeric species are observed after 24 h dialysis of the enzyme denatured with guanidine-HCl. Both the monomeric and dimeric forms recovered after dialysis are active

Sus scrofa

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653037