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Information on EC 3.5.2.5 - allantoinase and Organism(s) Escherichia coli and UniProt Accession P77671

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.2 In cyclic amides
                3.5.2.5 allantoinase
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This record set is specific for:
Escherichia coli
UNIPROT: P77671 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
allantoinase, allase, aln-1, allbali, osaln, metal-independent allantoinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
allantoinase
-
Fe-allantoinase
-
metal-dependent allantoinase
-
zinc-amended allantoinase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-allantoin amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-20-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-allantoin + H2O
allantoate
show the reaction diagram
(S)-allantoin + H2O
allantoate
show the reaction diagram
additional information
?
-
no substrate: hydantoin, dihydrouracil, phthalimide, dihydroorotate, and 3-imonoisoindolinone
-
-
?
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
(S)-allantoin + H2O
allantoate
show the reaction diagram
final step of ureide pathway
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
competitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
28.6 - 91.3
(S)-allantoin
5.5 - 79.9
(S)-allantoin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.237 - 0.795
dithiothreitol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.3
Ni2+-activated enzyme, pH 8.0, 25°C
2.6
Zn2+-activated enzyme, pH 8.0, 25°C
410
-
pH 7.4, 37°C, Co2+-amended culture
76.1
-
pH 7.4, 37°C, Zn2+-amended culture
8
Co2+-activated enzyme, pH 8.0, 25°C
88.2
Mn2+-activated enzyme, pH 8.0, 25°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
Mn2+-activited enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
189500
gel filtration
57150
gel filtration
93600
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
-
additional information
gel filtration chromatography reveals a mixture of monomers, dimers, and tetramers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D315N
no activity
N94D
no activity
N94V
no activity
R215K
no significant effect on enzyme activity
S288D
no significant effect on enzyme activity
S288V
no significant effect on enzyme activity
S317D
no activity
S317V
no activity
D315A
complete loss of activity
H186A
complete loss of activity
H242A
complete loss of activity
H59A
complete loss of activity
H61A
complete loss of activity
K146A
complete loss of activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
30 min, comnplete loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overproduction of enzyme in Escherichia coli
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
purified recombinant ALLase exhibits no activity but can be activated when preincubating with some metal ions before analyzing its activity. Renaturation follows in decreasing order Mn2+, Co2+, Zn2+, Ni2+, Cd2+, Mg2+
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mulrooney, S.B.; Hausinger, R.P.
Metal ion dependence of recombinant Escherichia coli allantoinase
J. Bacteriol.
185
126-134
2003
Escherichia coli
Manually annotated by BRENDA team
Kim, K.; Kim, M.I.; Chung, J.; Ahn, J.H.; Rhee, S.
Crystal structure of metal-dependent allantoinase from Escherichia coli
J. Mol. Biol.
387
1067-1074
2009
Escherichia coli (P77671), Escherichia coli
Manually annotated by BRENDA team
Ho, Y.Y.; Hsieh, H.C.; Huang, C.Y.
Biochemical characterization of allantoinase from Escherichia coli BL21
Protein J.
30
384-394
2011
Escherichia coli (A0A140NCJ5)
Manually annotated by BRENDA team