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Literature summary extracted from

  • Martinez-Gomez, A.I.; Soriano-Maldonado, P.; Andujar-Sanchez, M.; Clemente-Jimenez, J.M.; Rodriguez-Vico, F.; Neira, J.L.; Las Heras-Vazquez, F.J.; Martinez-Rodriguez, S.
    Biochemical and mutational studies of allantoinase from Bacillus licheniformis CECT 20T (2014), Biochimie, 99, 178-188.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.2.5 gene pucH, DNA and amino acid sequence determination and analysis, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3) Bacillus licheniformis

Protein Variants

EC Number Protein Variants Comment Organism
3.5.2.5 D319A site-directed mutagenesis, inactive mutant, altered thermal denaturation compared to the wild-type enzyme Bacillus licheniformis
3.5.2.5 D319N site-directed mutagenesis, inactive mutant, altered thermal denaturation compared to the wild-type enzyme Bacillus licheniformis
3.5.2.5 S292A site-directed mutagenesis, the mutant shows reduced activity and altered thermal denaturation compared to the wild-type enzyme Bacillus licheniformis
3.5.2.5 T155A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Bacillus licheniformis
3.5.2.5 T155Y site-directed mutagenesis, the mutant shows reduced activity and altered thermal denaturation compared to the wild-type enzyme Bacillus licheniformis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.2.5 8-Hydroxyquinoline-5-sulfonic acid complete inhibition Bacillus licheniformis
3.5.2.5 Acetohydroxamic acid
-
 Bacillus licheniformis
3.5.2.5 DTT complete inhibition Bacillus licheniformis
3.5.2.5 H2O2 allosteric effect of H2O2 toward allantoinase Bacillus licheniformis
3.5.2.5 L-cysteine complete inhibition Bacillus licheniformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.2.5 17.7
-
 (S)-allantoin pH 7.5, 50°C, recombinant wild-type enzyme Bacillus licheniformis
3.5.2.5 20.3
-
 (S)-allantoin pH 7.5, 50°C, recombinant mutant T155Y Bacillus licheniformis
3.5.2.5 20.9
-
 (S)-allantoin pH 7.5, 50°C, recombinant mutant T155A Bacillus licheniformis
3.5.2.5 35.7
-
 (S)-allantoin pH 7.5, 50°C, recombinant mutant S292A Bacillus licheniformis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.2.5 Co2+ activates, most effective metal cofactor, inverting the enantioselectivity of AllBali Bacillus licheniformis
3.5.2.5 Mn2+ activates Bacillus licheniformis
3.5.2.5 Zn2+ activates slightly Bacillus licheniformis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.2.5 170000 215000 gel filtration 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
-
 allantoate
-
 ?
3.5.2.5 (S)-allantoin + H2O Bacillus licheniformis CECT 20T
-
 allantoate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.5 Bacillus licheniformis L0CR34 gene pucH
-
3.5.2.5 Bacillus licheniformis CECT 20T L0CR34 gene pucH
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.2.5 recombinant wild-type and mutant His-tagged enzymes from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography, gel fltration, and ultrafiltration Bacillus licheniformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.2.5 (S)-allantoin + H2O
-
 Bacillus licheniformis allantoate
-
 ?
3.5.2.5 (S)-allantoin + H2O best substrate, enantioselectivity of Co2+-enzyme toward allantoin enantiomers Bacillus licheniformis allantoate
-
 ?
3.5.2.5 (S)-allantoin + H2O
-
 Bacillus licheniformis CECT 20T allantoate
-
 ?
3.5.2.5 (S)-allantoin + H2O best substrate, enantioselectivity of Co2+-enzyme toward allantoin enantiomers Bacillus licheniformis CECT 20T allantoate
-
 ?
3.5.2.5 5-ethyl-hydantoin + H2O low activity Bacillus licheniformis ?
-
 ?
3.5.2.5 5-ethyl-hydantoin + H2O low activity Bacillus licheniformis CECT 20T ?
-
 ?
3.5.2.5 dihydrouracil + H2O low activity Bacillus licheniformis ?
-
 ?
3.5.2.5 dihydrouracil + H2O low activity Bacillus licheniformis CECT 20T ?
-
 ?
3.5.2.5 hydantoin + H2O low activity Bacillus licheniformis ?
-
 ?
3.5.2.5 hydantoin + H2O low activity Bacillus licheniformis CECT 20T ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.2.5 homotetramer
-
 Bacillus licheniformis

Synonyms

EC Number Synonyms Comment Organism
3.5.2.5 allantoin amidohydrolase
-
 Bacillus licheniformis
3.5.2.5 AllBali
-
 Bacillus licheniformis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.2.5 50
-
-
 Bacillus licheniformis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.2.5 additional information
-
 apparent Tm of 62°C Bacillus licheniformis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.2.5 5.2
-
 (S)-allantoin pH 7.5, 50°C, recombinant mutant T155Y Bacillus licheniformis
3.5.2.5 10.1
-
 (S)-allantoin pH 7.5, 50°C, recombinant mutant T155A Bacillus licheniformis
3.5.2.5 24.4
-
 (S)-allantoin pH 7.5, 50°C, recombinant wild-type enzyme and mutant S292A Bacillus licheniformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.2.5 7.5
-
-
 Bacillus licheniformis

General Information

EC Number General Information Comment Organism
3.5.2.5 additional information residue Ser292 is likely implicated in the binding of the allantoin ring through the carbonyl group of the polypeptide main chain, which is the common mechanism observed in other members of the amidohydrolase family. Modeling and docking studies Bacillus licheniformis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.2.5 0.3
-
 (S)-allantoin pH 7.5, 50°C, recombinant mutant T155Y Bacillus licheniformis
3.5.2.5 0.5
-
 (S)-allantoin pH 7.5, 50°C, recombinant mutant T155A Bacillus licheniformis
3.5.2.5 0.7
-
 (S)-allantoin pH 7.5, 50°C, recombinant mutant S292A Bacillus licheniformis
3.5.2.5 1.4
-
 (S)-allantoin pH 7.5, 50°C, recombinant wild-type enzyme Bacillus licheniformis