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Literature summary for 3.4.21.53 extracted from

  • Maurizi, M.R.
    Degradation in vitro of bacteriophage lambda N protein by Lon protease from Escherichia coli (1987), J. Biol. Chem., 262, 2696-2703.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
adenosine 5'-(3-thiotriphosphate) i.e. adenosine 5'-O-(thiotriphosphate) or ATP-gamma-S, activation Escherichia coli
adenosine 5'-(3-thiotriphosphate) slight Escherichia coli
Adenyl-5'-yl imidodiphosphate can replace ATP Escherichia coli
Adenyl-5'-yl imidodiphosphate i.e. AMP-PNP, activation Escherichia coli
adenyl-5'-yl methylene diphosphonate i.e. AMP-PCP, activation Escherichia coli
adenyl-5'-yl methylene diphosphonate can replace ATP Escherichia coli
GTP not Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Denatured lambda Cro protein casein as substrate Escherichia coli
lambda-N-Protein casein as substrate Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Bacteriophage lambda N-protein + H2O Escherichia coli
-
?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Bacteriophage lambda N-protein + H2O
-
Escherichia coli ?
-
?
Bacteriophage lambda protein N + H2O cleavage sites: Ala16-Gln, Ala-Glu, Ala-Lys, Leu-Asn, Leu-Glu, Ser-Lys, Cys-Ser Escherichia coli Hydrolyzed bacteriophage lambda protein N
-
?
casein + H2O methylcasein Escherichia coli hydrolyzed casein
-
?
Denatured lambda Cro protein + H2O poor substrate, inhibits casein hydrolysis Escherichia coli ?
-
?
Glucagon + H2O cleavage sites: Leu6-Cys(SO3H), Leu17-Val, Ala14-Leu, Val18-Cys(SO3H) Escherichia coli Hydrolyzed glucagon
-
?
additional information cleavage specificity Escherichia coli ?
-
?
additional information No substrates are lambda-repressors cI and Cro, lambda replication protein O, E. coli galactose repressor, even after heat denaturation Escherichia coli ?
-
?
Oxidized insulin B-chain + H2O cleavage sites Escherichia coli Hydrolyzed insulin B-chain
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0333
-
casein
-
Escherichia coli
0.333
-
oxidized insulin B-chain
-
Escherichia coli
1
-
bacteriophage lambda N-protein
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP requirement Escherichia coli
ATP ATP-dependent protease Escherichia coli
CTP activation Escherichia coli
CTP less efficient than ATP Escherichia coli
UTP activation Escherichia coli
UTP less efficient than ATP Escherichia coli