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Literature summary for 3.1.1.45 extracted from

  • Pathak, D.; Ashley, G.; Ollis, D.
    Thiol protease-like active site found in the enzyme dienelactone hydrolase: localization using biochemical, genetic, and structural tools (1991), Proteins Struct. Funct. Genet., 9, 267-279.
    View publication on PubMed
Search for more literature for 3.1.1.45

Crystallization (Commentary)

Crystallization (Comment) Organism
refined crystal structure of DLH at 1.8 A, C123S DLH at 2.2 A, C123A at 2.0 A resolution Pseudomonas knackmussii

Protein Variants

Protein Variants Comment Organism
C123A inactive Pseudomonas knackmussii
C123S burst kinetics with p-nitrophenyl acetate, 10% as active as DLH Pseudomonas knackmussii
C60S no reduction in activity Pseudomonas knackmussii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.17
-
 trans-4-Carboxymethylenebut-2-en-4-olide
-
 Pseudomonas knackmussii
0.22
-
 trans-4-Carboxymethylenebut-2-en-4-olide C60S DLH Pseudomonas knackmussii
9.9
-
 trans-4-Carboxymethylenebut-2-en-4-olide C123S DLH Pseudomonas knackmussii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-carboxymethylenebut-2-en-4-olide + H2O Pseudomonas knackmussii the enzyme is one of the enzymes of the halocatechol branch of the beta-ketoadipate pathway, a complex set of catabolic reactions used by bacteria for utilization of aromatic compounds ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas knackmussii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
3-chlorobenzoate-grown cells Pseudomonas knackmussii
C123A DLH Pseudomonas knackmussii
C123S DLH Pseudomonas knackmussii

Reaction

Reaction Comment Organism Reaction ID
4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate mechanism Pseudomonas knackmussii
a
4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate esterase activity on chromophoric ester substrate, p-nitrophenyl acetate and the synthetic active-site titrant, trans-cinnamoyl imidazole Pseudomonas knackmussii
a
4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate the active-site Cys123 residue is part of a triad of residues consisting of Cys123, His202 and Asp171, and is reminiscent of the serine/cysteine proteases Pseudomonas knackmussii
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-carboxymethylenebut-2-en-4-olide + H2O the enzyme is one of the enzymes of the halocatechol branch of the beta-ketoadipate pathway, a complex set of catabolic reactions used by bacteria for utilization of aromatic compounds Pseudomonas knackmussii ?
-
 ?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
-
 Pseudomonas knackmussii 4-oxohex-2-enedioate
-
 ?
p-nitrophenyl acetate + H2O esterase activity Pseudomonas knackmussii p-nitrophenol + acetate
-
 ?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
-
 Pseudomonas knackmussii 4-oxohex-2-enedioate
-
 ?
trans-cinnamoyl imidazole + H2O esterase activity Pseudomonas knackmussii trans-cinnamate + imidazole
-
 ?

Subunits

Subunits Comment Organism
monomer alpha,beta protein Pseudomonas knackmussii

Synonyms

Synonyms Comment Organism
DLH
-
 Pseudomonas knackmussii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.67
-
 trans-4-Carboxymethylenebut-2-en-4-olide C123S DLH Pseudomonas knackmussii
9.17
-
 trans-4-Carboxymethylenebut-2-en-4-olide
-
 Pseudomonas knackmussii
15
-
 trans-4-Carboxymethylenebut-2-en-4-olide C60S DLH Pseudomonas knackmussii