Native Achromobacter lyticus Achromopeptidase

Names

[ Name ]:
Native Achromobacter lyticus Achromopeptidase

[Synonym ]:
Achromobacter protease I
Achromobacter proteinase I
Achromopeptidase
E.C. 3.4.21.50
Endo-Lys-C protease
Endopeptidase Lys-C
Endoprotease LysC
Endoproteinase Lys-C
Native Achromobacter lyticus Achromopeptidase

Biological Activity

[Description]:

Lysyl endopeptidase (Lys-C) catalyzes carboxyl oxygen exchange reaction. Lysyl endopeptidase has higher substrate binding affinities and higher catalytic rates at the acidic pHs than at the alkaline pHs[1].

[Related Catalog]:

Research Areas >> Others

Signaling Pathways >> Others >> Others

[References]

[1]. Hajkova D, et al. pH dependency of the carboxyl oxygen exchange reaction catalyzed by lysyl endopeptidase and trypsin. J Proteome Res. 2006 Jul;5(7):1667-73.

Chemical & Physical Properties

No Any Chemical & Physical Properties

Safety Information

[ Symbol ]:

GHS08

[ Signal Word ]:
Danger

[ Hazard Statements ]:
H334

[ Precautionary Statements ]:
P261-P342 + P311

[ Personal Protective Equipment ]:
dust mask type N95 (US);Eyeshields;Faceshields;Gloves

[ Hazard Codes ]:
Xn

[ Risk Phrases ]:
42/43-42

[ RIDADR ]:
NONH for all modes of transport

[ WGK Germany ]:
3

Articles

Probing PrPSc structure using chemical cross-linking and mass spectrometry: evidence of the proximity of Gly90 amino termini in the PrP 27-30 aggregate.

Biochemistry 44(30) , 10100-9, (2005)

Elucidation of the structure of PrP(Sc) continues to be one of the most important and difficult challenges in prion research. This task, essential for gaining an understanding of the basis of prion in...

Analysis of the peptidoglycan hydrolase complement of Lactobacillus casei and characterization of the major γ-D-glutamyl-L-lysyl-endopeptidase.

PLoS ONE 7(2) , e32301, (2012)

Peptidoglycan (PG) is the major component of Gram positive bacteria cell wall and is essential for bacterial integrity and shape. Bacteria synthesize PG hydrolases (PGHs) which are able to cleave bond...

Identification of the epsilon-(gamma-glutamyl)lysine cross-linking sites in alpha-lactalbumin polymerized by mammalian and microbial transglutaminases.

J. Agric. Food Chem. 50(25) , 7412-9, (2002)

To investigate the site specificity of two transglutaminases (TGases), that is, the enzymes from guinea pig liver (GTGase) and Streptoverticillium (MTGase), the acyl acceptor and donor sites in alpha-...