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Literature summary for 1.14.11.56 extracted from

  • Meyer, F.; Frey, R.; Ligibel, M.; Sager, E.; Schroer, K.; Snajdrova, R.; Buller, R.
    Modulating chemoselectivity in a Fe(II)/alpha-ketoglutarate-dependent dioxygenase for the oxidative modification of a nonproteinogenic amino acid (2021), ACS Catal., 11, 6261-6269 .
No PubMed abstract available
Search for more literature for 1.14.11.56

Protein Variants

Protein Variants Comment Organism
W40M acceptance of the native substrate L-proline is almost completely abolished. 8.3fold increase in turnover number for L-homophenylalanine as compared to wild-type enzyme. Mutation reprograms the natural hydroxylase to predominantly act as a desaturase, giving almost exclusively 3,4-desaturated L-homophenylalanine, through capability of tyrosine to serve as a catalytic entity in the reaction mechanism Sinorhizobium meliloti
W40M/I103L acceptance of the native substrate L-proline is almost completely abolished. 112fold increase in turnover number for L-homophenylalanine and and about 300fold improved kcat/Km compared to the wild-type enzyme Sinorhizobium meliloti

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.24
-
 L-homophenylalanine 20°C, pH not specified in the publication, mutant enzyme W40M Sinorhizobium meliloti
0.3
-
 L-homophenylalanine 20°C, pH not specified in the publication, mutant enzyme W40M/I103L Sinorhizobium meliloti
1.1
-
 L-homophenylalanine 20°C, pH not specified in the publication, wild-type enzyme Sinorhizobium meliloti

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ Fe2+-dependent enzyme Sinorhizobium meliloti

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-proline + 2-oxoglutarate + O2 Sinorhizobium meliloti
-
 cis-4-hydroxy-L-proline + succinate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti Q92LF6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-homophenylalanine + 2-oxoglutarate + O2 mutant enzyme W40M shows 8.3fold increase in turnover number for L-homophenylalanine as compared to wild-type enzyme and mutant enzyme W40M/I103L shows 112fold increase in turnover number. Mutation reprograms the natural hydroxylase to predominantly act as a desaturase, giving almost exclusively 3,4-desaturated L-homophenylalanine, through capability of tyrosine to serve as a catalytic entity in the reaction mechanism Sinorhizobium meliloti ? + succinate + CO2
-
 ?
L-proline + 2-oxoglutarate + O2
-
 Sinorhizobium meliloti cis-4-hydroxy-L-proline + succinate + CO2
-
 ?
L-proline + 2-oxoglutarate + O2 acceptance of the native substrate L-proline is almost completely abolished in the mutant enzymes W40M und W40M/I103L Sinorhizobium meliloti cis-4-hydroxy-L-proline + succinate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
L-proline cis-4-hydroxylase
-
 Sinorhizobium meliloti
SmP4H
-
 Sinorhizobium meliloti

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00025
-
 L-homophenylalanine 20°C, pH not specified in the publication, wild-type enzyme Sinorhizobium meliloti
0.0021
-
 L-homophenylalanine 20°C, pH not specified in the publication, mutant enzyme W40M Sinorhizobium meliloti
0.028
-
 L-homophenylalanine 20°C, pH not specified in the publication, mutant enzyme W40M/I103L Sinorhizobium meliloti

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0002
-
 L-homophenylalanine 20°C, pH not specified in the publication, wild-type enzyme Sinorhizobium meliloti
0.0086
-
 L-homophenylalanine 20°C, pH not specified in the publication, mutant enzyme W40M Sinorhizobium meliloti
0.07
-
 L-homophenylalanine 20°C, pH not specified in the publication, mutant enzyme W40M/I103L Sinorhizobium meliloti