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

BRENDA support

Literature summary extracted from

  • Conejero-Muriel, M.; Martinez-Gomez, A.I.; Martinez-Rodriguez, S.; Gavira, J.A.
    Cloning, expression, purification, crystallization and preliminary X-ray characterization of allantoinase from Bacillus licheniformis ATCC 14580 (2014), Acta Crystallogr. Sect. F, 70, 1513-1516.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.2.5 recombinant overexpression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus licheniformis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.2.5 purified recombinant His6-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml 14 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 20% w/v PEG 3350, and 0.1 M potassium thiocyanate, pH 6.5, equilibration against 0.5 ml reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 3.5 A resolution Bacillus licheniformis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.2.5 51163
-
x * 51163, sequence calculation Bacillus licheniformis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.2.5 (S)-allantoin + H2O Bacillus licheniformis allantoinase catalyzes the reversible hydrolysis of allantoin into allantoate by hydrolytic cleavage of the N1-C2 amide bond of the five-membered hydantoin ring. The enzyme shows an inverted enantioselectivity towards allantoin, R-enantioselective allantoate
-
r
3.5.2.5 (S)-allantoin + H2O Bacillus licheniformis ATCC 14580 allantoinase catalyzes the reversible hydrolysis of allantoin into allantoate by hydrolytic cleavage of the N1-C2 amide bond of the five-membered hydantoin ring. The enzyme shows an inverted enantioselectivity towards allantoin, R-enantioselective allantoate
-
r

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.5 Bacillus licheniformis Q65LN0
-
-
3.5.2.5 Bacillus licheniformis ATCC 14580 Q65LN0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.2.5 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, ultrafiltration, and dialysis Bacillus licheniformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.2.5 (S)-allantoin + H2O allantoinase catalyzes the reversible hydrolysis of allantoin into allantoate by hydrolytic cleavage of the N1-C2 amide bond of the five-membered hydantoin ring. The enzyme shows an inverted enantioselectivity towards allantoin, R-enantioselective Bacillus licheniformis allantoate
-
r
3.5.2.5 (S)-allantoin + H2O allantoinase catalyzes the reversible hydrolysis of allantoin into allantoate by hydrolytic cleavage of the N1-C2 amide bond of the five-membered hydantoin ring. The enzyme shows an inverted enantioselectivity towards allantoin, R-enantioselective Bacillus licheniformis ATCC 14580 allantoate
-
r

Subunits

EC Number Subunits Comment Organism
3.5.2.5 ? x * 51163, sequence calculation Bacillus licheniformis

Synonyms

EC Number Synonyms Comment Organism
3.5.2.5 AllBali
-
Bacillus licheniformis