3.5.2.7: imidazolonepropionase
This is an abbreviated version!
For detailed information about imidazolonepropionase, go to the full flat file.
Word Map on EC 3.5.2.7
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3.5.2.7
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subtilis
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cytosine
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agrobacterium
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tumefaciens
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carbon-nitrogen
- 3.5.2.7
- subtilis
- cytosine
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agrobacterium
- tumefaciens
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carbon-nitrogen
Reaction
Synonyms
4-imidazolone-5-propanoate amidohydrolase, HutI, imidazolone-5-propanoate hydrolase, Imidazolone-5-propionate hydrolase, imidazolonepropionase
ECTree
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General Information
General Information on EC 3.5.2.7 - imidazolonepropionase
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metabolism
additional information
imidazolonepropionase (HutI) catalyzes the hydrolytic cleavage of carbon-nitrogen bond in 4-imidazolone-5-propionic acid (IPA) to yield L-formiminoglutamic acid, which is the third step in the universal histidine degradation pathway
metabolism
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imidazolonepropionase (HutI) catalyzes the hydrolytic cleavage of carbon-nitrogen bond in 4-imidazolone-5-propionic acid (IPA) to yield L-formiminoglutamic acid, which is the third step in the universal histidine degradation pathway
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catalytic mechanism, modeling, optimized structures of transition states and intermediates, combined quantum mechanics and molecular mechanics (QM/MM) calculations and modeling, overview. Activation of hydrolytic water (a zinc-bound water) is performed by residue E252 via a bridging water molecule, which occurs before binding of the substrate. After the substrate binding, this activation channel is blocked by the substrate, and the other two residues (D324 and H272) cannot act as the general base to activate the hydrolytic water. For the two (S)-enantiomers of IPA, HutI can specifically convert one isomer of (S)-enantiomer (SIPA-1) to l-formiminoglutamic acid
additional information
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catalytic mechanism, modeling, optimized structures of transition states and intermediates, combined quantum mechanics and molecular mechanics (QM/MM) calculations and modeling, overview. Activation of hydrolytic water (a zinc-bound water) is performed by residue E252 via a bridging water molecule, which occurs before binding of the substrate. After the substrate binding, this activation channel is blocked by the substrate, and the other two residues (D324 and H272) cannot act as the general base to activate the hydrolytic water. For the two (S)-enantiomers of IPA, HutI can specifically convert one isomer of (S)-enantiomer (SIPA-1) to l-formiminoglutamic acid
additional information
-
catalytic mechanism, modeling, optimized structures of transition states and intermediates, combined quantum mechanics and molecular mechanics (QM/MM) calculations and modeling, overview. Activation of hydrolytic water (a zinc-bound water) is performed by residue E252 via a bridging water molecule, which occurs before binding of the substrate. After the substrate binding, this activation channel is blocked by the substrate, and the other two residues (D324 and H272) cannot act as the general base to activate the hydrolytic water. For the two (S)-enantiomers of IPA, HutI can specifically convert one isomer of (S)-enantiomer (SIPA-1) to l-formiminoglutamic acid
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