3.5.4.10: IMP cyclohydrolase

This is an abbreviated version!
For detailed information about IMP cyclohydrolase, go to the full flat file.

Word Map on EC 3.5.4.10

Reaction

IMP
+
H2O
=
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide

Synonyms

inosinicase, inosinate cyclohydrolase, IMPCHase, inosine monophosphate cyclohydrolase, ATIC, IMP synthetase, IMPCH, PurH, inosine 5'-monophosphate cyclohydrolase, MthPurO, PurO, MjPurO, AICAR transformylase/inosine 5'-monophosphate cyclohydrolase, AICAR-FT/IMP-CHase, ITGA2, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase, 5-aminoimidazole-4-carboxamide ribonucleotide tranformylase/IMP cyclohydrolase, AICAR tranformylase/IMP cyclohydrolase, AICAR-transformylase/IMP cyclohydrolase, atic-1, AICAR transformylase/IMP cyclohydrolase, TK0430, PurO-type IMP cyclohydrolase, PurH2, AF1811, PurH2-type IMP cyclohydrolase

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.4 In cyclic amidines
                3.5.4.10 IMP cyclohydrolase

Engineering

Engineering on EC 3.5.4.10 - IMP cyclohydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D125A
D125N
D125E
K137A
Y104A
Y104F
K137R
Y104A/D125A
Y104F/D125A
K246R
natural mutation observed in female infant patient with lack in transformylase activity and about 40% residual enzymic activity, showing massive excretion of 5-amino-4-imidazolecarboxamide riboside, dysmorphic features, severe neurological defects, and congenital blindness. Recombinant protein with K426R mutation completely lacks AICAR transformylase activity
C807T
-
naturally occuring polymorphism involved in gastric cancer development
R31K
site-directed mutagenesis, the mutant shows 76% reduced activity compared to the wild-type enzyme
C61A
site-directed mutagenesis, the mutant shows 8fold increased activity compared to the wild-type enzyme
Y59F
site-directed mutagenesis, the mutant shows 34% reduced activity compared to the wild-type enzyme
E102Q
site-directed mutagenesis, inactive mutant
H256A
complete loss of activity, mutation lowers the thermostability
K255A
complete loss of activity, mutation lowers the thermostability
K255R
mutation reduces activity by 76%. Mutation increases the Tm by approximately 3°C
N415A
decrease in AICAR transformylase activity as compared with wild-type SlugATIC, indicating it might also play essential role in substrate binding. Increase in the thermostability