A7550
Achromopeptidase from Achromobacter lyticus
lyophilized powder, Protein ~5 % by biuret, 300-600 units/mg solid
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About This Item
CAS Number:
UNSPSC Code:
12352204
MDL number:
form
lyophilized powder
specific activity
300-600 units/mg solid
composition
Protein, ~5% biuret
foreign activity
Collagenase, present
storage temp.
−20°C
Biochem/physiol Actions
Achromopeptidase is a lysyl endopeptidase with a MW of ~27 kDa. It is useful for lysis of Gram-positive bacteria that are resistant to lysozyme.
pH Optimum for activity: pH 8.5 - 9
Approximately 500-1,500 un/ml achromopetidase can be used to lyse cells at a density of OD600=0.6 over 2 hours at 37 °C.
pH Optimum for activity: pH 8.5 - 9
Approximately 500-1,500 un/ml achromopetidase can be used to lyse cells at a density of OD600=0.6 over 2 hours at 37 °C.
Physical form
Crude powder containing salts and medium components
Other Notes
One unit will produce a change in A600 of 0.001 per minute per mL at pH 8.0 at 37 °C using a suspension of Micrococcus lysodeikticus as substrate (1 cm light path).
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Beatrice Quevedo et al.
BMC microbiology, 11, 14-14 (2011-01-21)
The purpose of this study was to design and evaluate fluorescent in situ hybridization (FISH) probes for the single-cell detection and enumeration of lactic acid bacteria, in particular organisms belonging to the major phylogenetic groups and species of oral lactobacilli
Niamh Toomey et al.
Applied and environmental microbiology, 75(10), 3146-3152 (2009-03-10)
Three wild-type dairy isolates of lactic acid bacteria (LAB) and one Lactococcus lactis control strain were analyzed for their ability to transfer antibiotic resistance determinants (plasmid or transposon located) to two LAB recipients using both in vitro methods and in
T Masaki et al.
Biochimica et biophysica acta, 660(1), 44-50 (1981-07-24)
Achromobacter lyticus M497-1 produces three kinds of alkaline proteases (protease I, II and III) in culture medium along with the bacteriolytic enzyme (Masaki, T., Nakamura, K., Isono, M. and Soejima, M. (1978) Agric. Biol. Chem. 42, 1443--1445). Among these three
T Masaki et al.
Biochimica et biophysica acta, 660(1), 51-55 (1981-07-24)
The unique specificity of Achromobacter protease I for lysine residue was investigated using synthetic and natural substrates, i.e., lysine derivatives, arginine derivatives, lysine vasopressin, substance P, ACTH and insulin. The enzyme cleaved only the -Lys-X- bonds in the above substrates.
pH dependency of the carboxyl oxygen exchange reaction catalyzed by lysyl endopeptidase and trypsin.
Dagmar Hajkova et al.
Journal of proteome research, 5(7), 1667-1673 (2006-07-11)
The pH dependency of the carboxyl oxygen exchange reaction catalyzed by lysyl endopeptidase (Lys-C) and trypsin has been studied. The reaction was quantitatively monitored by measuring the incorporation of 18O atom into the alpha-carboxyl group of N(alpha)-acetyl-L-lysine from H2(18)O solvent.
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