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Information on EC 3.5.99.2 - aminopyrimidine aminohydrolase and Organism(s) Bacillus subtilis and UniProt Accession P25052

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IUBMB Comments
Previously known as thiaminase II, this enzyme is involved in the regeneration of the thiamine pyrimidine from degraded products, rather than in thiamine degradation, and participates in thiamine salvage pathways.
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Bacillus subtilis
UNIPROT: P25052
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
thiaminase, thi20, thiaminase ii, thi20p, tena_c, thiaminase type ii, hp1287, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
thiaminase II
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thiaminase II
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-N bond
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
4-amino-5-aminomethyl-2-methylpyrimidine aminohydrolase
Previously known as thiaminase II, this enzyme is involved in the regeneration of the thiamine pyrimidine from degraded products, rather than in thiamine degradation, and participates in thiamine salvage pathways.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-80-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-amino-5-aminomethyl-2-methylpyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
show the reaction diagram
-
-
-
?
oxothiamin + H2O
?
show the reaction diagram
-
-
-
?
oxythiamin + H2O
?
show the reaction diagram
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-amino-5-aminomethyl-2-methylpyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
show the reaction diagram
-
-
-
?
oxothiamin + H2O
?
show the reaction diagram
-
-
-
?
oxythiamin + H2O
?
show the reaction diagram
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
show the reaction diagram
-
-
-
?
additional information
?
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no activity with N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine, thiamin monophosphate, thiamin diphosphate, thiamin disulfide, desthiothiamin, and thiochrome
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.091
with oxothiamin as substrate, at 30°C in 45 mM Tris/HCl buffer, pH 7.5, containing 0.9 mM dithiothreitol and 0.45 M glycinebetaine
0.162
with thiamine as substrate, at 30°C in 45 mM Tris/HCl buffer, pH 7.5, containing 0.9 mM dithiothreitol and 0.45 M glycinebetaine
0.205
with oxythiamin as substrate, at 30°C in 45 mM Tris/HCl buffer, pH 7.5, containing 0.9 mM dithiothreitol and 0.45 M glycinebetaine
0.292
with 4-amino-5-aminomethyl-2-methylpyrimidine as substrate, at 30°C in 45 mM Tris/HCl buffer, pH 7.5, containing 0.9 mM dithiothreitol and 0.45 M glycinebetaine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
x * 30000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 30000, SDS-PAGE
dimer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and gel filtration
Ni2+ -affinity column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIPL cells
expressed in Escherichia coli strain BL21(D3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Toms, A.V.; Haas, A.L.; Park, J.H.; Begley, T.P.; Ealick, S.E.
Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II
Biochemistry
44
2319-2329
2005
Bacillus subtilis (P25052), Bacillus subtilis
Manually annotated by BRENDA team
Zallot, R.; Yazdani, M.; Goyer, A.; Ziemak, M.J.; Guan, J.C.; McCarty, D.R.; de Crecy-Lagard, V.; Gerdes, S.; Garrett, T.J.; Benach, J.; Hunt, J.F.; Shintani, D.K.; Hanson, A.D.
Salvage of the thiamin pyrimidine moiety by plant TenA proteins lacking an active-site cysteine
Biochem. J.
463
145-155
2014
Bacillus subtilis (P25052), Bacillus subtilis 168 (P25052)
Manually annotated by BRENDA team