Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.1.87 extracted from

  • Nandanwar, H.; Vohra, R.; Hoondal, G.
    Enhanced stability of newly isolated trimeric L-methionine-N-carbamoylase from Brevibacillus reuszeri HSN1 by covalent immobilization (2013), Biotechnol. Appl. Biochem., 60, 305-315.
    View publication on PubMed
Search for more literature for 3.5.1.87

Application

Application Comment Organism
additional information immobilization of the enzyme by covalent coupling to a solid support material including additional cross-linking with polyaldehyde-dextran, method development, overview. Temperature and pH optima of immobilized enzyme are increased by 10°C and 0.5 unit, respectively. The enzyme is significantly stabilized, it is recycled nine times with about 100% conversion efficiency when batch experiments are carried out at 35°C, pH 7.5, for the 180 min cycle Brevibacillus reuszeri

Protein Variants

Protein Variants Comment Organism
additional information immobilization of the enzyme by covalent coupling to a solid support material including additional cross-linking with polyaldehyde-dextran, method development, overview. Temperature and pH optima of immobilized enzyme are increased by 10°C and 0.5 unit, respectively. The enzyme is significantly stabilized, it is recycled nine times with about 100% conversion efficiency when batch experiments are carried out at 35°C, pH 7.5, for the 180 min cycle Brevibacillus reuszeri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
17.8
-
 N-carbamoyl-L-methionine pH 7.5, 40°C Brevibacillus reuszeri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-carbamoyl-L-methionine + H2O Brevibacillus reuszeri
-
 L-methionine + CO2 + NH3
-
 ?
N-carbamoyl-L-methionine + H2O Brevibacillus reuszeri HSN1
-
 L-methionine + CO2 + NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Brevibacillus reuszeri
-
-
-
Brevibacillus reuszeri HSN1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 60fold to homogeneity by heat treatment at 70°C for 2 min, anion exchange chromatography of the supernatant, hydrophobic interaction chromatography, ultrafiltration, and gel filtration Brevibacillus reuszeri

Storage Stability

Storage Stability Organism
4°C, the immobilized enzyme retaines approximately 50% of its activity after 5 months, while the free enzyme loses the complete enzyme activity with a half-life of 12 days Brevibacillus reuszeri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-carbamoyl-L-methionine + H2O
-
 Brevibacillus reuszeri L-methionine + CO2 + NH3
-
 ?
N-carbamoyl-L-methionine + H2O preferred substrate Brevibacillus reuszeri L-methionine + CO2 + NH3
-
 ?
N-carbamoyl-L-methionine + H2O
-
 Brevibacillus reuszeri HSN1 L-methionine + CO2 + NH3
-
 ?
N-carbamoyl-L-methionine + H2O preferred substrate Brevibacillus reuszeri HSN1 L-methionine + CO2 + NH3
-
 ?

Subunits

Subunits Comment Organism
homotrimer
-
 Brevibacillus reuszeri

Synonyms

Synonyms Comment Organism
L-methionine-N-carbamoylase
-
 Brevibacillus reuszeri
L-N-carbamoylase
-
 Brevibacillus reuszeri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 free enzyme Brevibacillus reuszeri

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 the immobilized enzyme retains about 93% activity after 60 min, at pH 7.5, whereas the free enzyme loses about 50% activity Brevibacillus reuszeri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 free enzyme Brevibacillus reuszeri