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Literature summary extracted from

  • Meshach Paul, D.; Chadah, T.; Senthilkumar, B.; Sethumadhavan, R.; Rajasekaran, R.
    Structural distortions due to missense mutations in human formylglycine-generating enzyme leading to multiple sulfatase deficiency (2017), J. Biomol. Struct. Dyn., 36, 3575-3585.
    View publication on PubMed

Application

EC Number Application Comment Organism
5.1.2.2 additional information mandelate racemase from Pseudomonas putida is a promising candidate for the dynamic kinetic resolution of alpha-hydroxy carboxylic acids Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.8.3.7 A177P the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 A279V the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 A348P the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 C218Y the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 C336R the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 E130D the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 N259I the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 P266L the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 R224W the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 R345C the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 R349Q the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 R349W the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 S155P the mutation is associated with multiple sulfatase deficiency Homo sapiens
1.8.3.7 W179S the mutation is associated with multiple sulfatase deficiency Homo sapiens
5.1.2.2 additional information evaluation of design of mandelate racemase with higher stability, usage of structural enzyme analysis for reengineering of mandelate racemase for enhanced thermal stability Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.3.7 a [sulfatase]-L-cysteine + O2 + a thiol Homo sapiens
-
 a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
 ?
5.1.2.2 (S)-mandelate Pseudomonas putida
-
 (R)-mandelate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.7 Homo sapiens
-
-
-
5.1.2.2 Pseudomonas putida P11444
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.7 a [sulfatase]-L-cysteine + O2 + a thiol
-
 Homo sapiens a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
 ?
5.1.2.2 (S)-mandelate
-
 Pseudomonas putida (R)-mandelate
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.8.3.7 FGE
-
 Homo sapiens
5.1.2.2 mdlA
-
 Pseudomonas putida

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.2.2 additional information
-
 the thermal stability of mandelate racemase is investigated through molecular dynamics simulations in the temperature range of 30-90°C, structural alterations at increasing temperatures, overview. Radius of gyration, surface accessibility, and secondary structure content suggest the instability of mandelate racemase at high temperatures Pseudomonas putida

General Information

EC Number General Information Comment Organism
1.8.3.7 malfunction structural distortions due to missense mutations in human formylglycine-generating enzyme lead to multiple sulfatase deficiency Homo sapiens
5.1.2.2 additional information the thermal stability of mandelate racemase is investigated through molecular dynamics simulations in the temperature range of 30-90°C Pseudomonas putida