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Literature summary for 3.8.1.10 extracted from

  • Nakamura, T.; Yamaguchi, A.; Kondo, H.; Watanabe, H.; Kurihara, T.; Esaki, N.; Hirono, S.; Tanaka, S.
    Roles of K151 and D180 in L-2-haloacid dehalogenase from Pseudomonas sp. YL: Analysis by molecular dynamics and ab initio fragment molecular orbital calculations (2009), J. Comput. Chem., 30, 2625-2634.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D180A the mutation destabilizes the rotation of the nucleophile D10, fixes catalytic water around D10, and prevents K151 from approaching D10 Pseudomonas sp.
K151A the mutant is almost inactive, the mutation destabilizes substrate orientation and affects the balance of the charge around the active site Pseudomonas sp.
K151R the mutant is almost inactive Pseudomonas sp.
S118A the mutant retains 30% of the activity of the wild type enzyme Pseudomonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-2-chloropropionate + H2O Pseudomonas sp.
-
D-lactate + HCl
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-2-haloacid + H2O
-
Pseudomonas sp. (S)-2-hydroxyacid + halide
-
?
(S)-2-haloacid + H2O
-
Pseudomonas sp. (R)-2-hydroxyacid + halide
-
?
L-2-chloropropionate + H2O
-
Pseudomonas sp. D-lactate + HCl
-
?

Synonyms

Synonyms Comment Organism
L-2-haloacid dehalogenase
-
Pseudomonas sp.
L-DEX YL
-
Pseudomonas sp.