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Literature summary for 3.5.2.7 extracted from

  • Su, H.; Sheng, X.; Liu, Y.
    Exploring the substrate specificity and catalytic mechanism of imidazolonepropionase (HutI) from Bacillus subtilis (2016), Phys. Chem. Chem. Phys., 18, 27928-27938 .
    View publication on PubMed
Search for more literature for 3.5.2.7

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information determination of reaction thermodynamics Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ enzyme-bound Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O Bacillus subtilis
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 N-formimidoyl-L-glutamate + H+
-
 ?
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O Bacillus subtilis 168
-
 N-formimidoyl-L-glutamate + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P42084
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-
Bacillus subtilis 168 P42084
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O
-
 Bacillus subtilis N-formimidoyl-L-glutamate + H+
-
 ?
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O
-
 Bacillus subtilis 168 N-formimidoyl-L-glutamate + H+
-
 ?
additional information analysis of substrate specificity and catalytic mechanism of imidazolonepropionase considering the four isomers of (S)- and (R)-enantiomers of 4-imidazolone-5-propionic acid (SIPA-1, SIPA-2, RIPA-1 and RIPA-2), overview. SIPA-1 is suggested to be the most favorable substrate for HutI, whereas the hydrolytic cleavage of SIPA-2 may require a preliminary isomerization to SIPA-1 Bacillus subtilis ?
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additional information analysis of substrate specificity and catalytic mechanism of imidazolonepropionase considering the four isomers of (S)- and (R)-enantiomers of 4-imidazolone-5-propionic acid (SIPA-1, SIPA-2, RIPA-1 and RIPA-2), overview. SIPA-1 is suggested to be the most favorable substrate for HutI, whereas the hydrolytic cleavage of SIPA-2 may require a preliminary isomerization to SIPA-1 Bacillus subtilis 168 ?
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-

Synonyms

Synonyms Comment Organism
HutI
-
 Bacillus subtilis
imidazolonepropionase
-
 Bacillus subtilis

General Information

General Information Comment Organism
metabolism 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 Bacillus subtilis
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 Bacillus subtilis