3.5.2.16: maleimide hydrolase
This is an abbreviated version!
For detailed information about maleimide hydrolase, go to the full flat file.
Word Map on EC 3.5.2.16
-
3.5.2.16
-
hydantoinase
-
dihydropyrimidinase
-
allantoinase
-
hydantoin
-
dihydroorotase
-
succinimide
-
dihydrouracil
-
blastobacter
-
phthalimide
-
monoamidated
-
3.5.2.2
-
glutarimide
-
putida
-
alcaligenes
-
dicarboxylate
-
metalloenzymes
-
lineweaver-burk
-
eutrophus
-
flavonols
-
l-amino
-
galangin
-
dimer-dimer
-
sulfur-containing
-
kaempferol
-
rhodanine
-
patchdock
-
binuclear
-
dihydrothymine
-
copurification
-
hydrase
-
amidases
-
octyl
-
allantoin
-
amidohydrolases
-
2,4-thiazolidinedione
- 3.5.2.16
- hydantoinase
- dihydropyrimidinase
- allantoinase
- hydantoin
- dihydroorotase
- succinimide
- dihydrouracil
- blastobacter
- phthalimide
-
monoamidated
-
3.5.2.2
- glutarimide
- putida
- alcaligenes
- dicarboxylate
-
metalloenzymes
-
lineweaver-burk
- eutrophus
- flavonols
-
l-amino
- galangin
-
dimer-dimer
-
sulfur-containing
- kaempferol
- rhodanine
-
patchdock
-
binuclear
- dihydrothymine
-
copurification
-
hydrase
- amidases
-
octyl
- allantoin
-
amidohydrolases
- 2,4-thiazolidinedione
Reaction
Synonyms
CIH, cyclic imide hydrolase, cyclic-imide amidohydrolase (decyclicizing), imidase
ECTree
Advanced search results
Engineering
Engineering on EC 3.5.2.16 - maleimide hydrolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
C108G
72% of wild-type activity. Like wild-type, mutant forms tetramers. It has a high binding ability for Zn2+
C7G
complete loss of activity. Mutant is a mixture of monomers and oligomers and displays decreased binding of Zn2+
C7G/C108G
H247A
-
decrease in absorbance at 500 nm by 32.4%. Less than 10% of wild-type activity
H86A
-
decrease in absorbance at 500 nm by 14.7%. Less than 10% of wild-type activity
C108G
-
72% of wild-type activity. Like wild-type, mutant forms tetramers. It has a high binding ability for Zn2+
-
C7G
-
complete loss of activity. Mutant is a mixture of monomers and oligomers and displays decreased binding of Zn2+
-
C7G/C108G
H247A
-
decrease in absorbance at 500 nm by 32.4%. Less than 10% of wild-type activity
-
H86A
-
decrease in absorbance at 500 nm by 14.7%. Less than 10% of wild-type activity
-
-
decrease in absorbance at 500 nm by 12.8%. Less than 10% of wild-type activity
C7G/C108G
complete loss of activity. Mutants is a multimer, with decreased binding ability for Zn2+
-
decrease in absorbance at 500 nm by 12.8%. Less than 10% of wild-type activity
-
C7G/C108G
-
complete loss of activity. Mutants is a multimer, with decreased binding ability for Zn2+
-