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5.3.2.5: 2,3-diketo-5-methylthiopentyl-1-phosphate enolase

This is an abbreviated version!
For detailed information about 2,3-diketo-5-methylthiopentyl-1-phosphate enolase, go to the full flat file.

Word Map on EC 5.3.2.5

Reaction

5-(methylsulfanyl)-2,3-dioxopentyl phosphate
=
2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate

Synonyms

2,3-diketo-5-methylthiopentane 1-phosphate enolase, DK-MTP 1-P enolase, DK-MTP-1-P enolase, DKMTP-1-P enolase, DKMTP-1P enolase, MtnBD, MtnW, ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein, RLP, RuBisCO-like protein, YkrW

ECTree

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.2 Interconverting keto- and enol-groups
                5.3.2.5 2,3-diketo-5-methylthiopentyl-1-phosphate enolase

Engineering

Engineering on EC 5.3.2.5 - 2,3-diketo-5-methylthiopentyl-1-phosphate enolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K122E
-
the mutant fails to form a catalytic dimer and does not show any DK-MTP-1-P enolase activity
K122M
-
the mutant fails to form a catalytic dimer and does not show any DK-MTP-1-P enolase activity
K122R
-
the mutant has specific activity of 32% less than that of the wild type enzyme and a lower thermal stability than the wild type enzyme
K147A
site-directed mutagenesis, the mutant requires a 10fold greater concentration of protein for enolization of the natural substrate, reduced activity compared to the wild-type enzyme
K173A
site-directed mutagenesis, the mutant is able to catalyze enolization at approximately the same rate as the wild-type enzyme
K98A
site-directed mutagenesis, the mutant is unable to catalyze the enolase reaction
additional information
-
a growth-defective mutant, in which the gene for the RLP is disrupted, is rescued by the gene for RuBisCO from the photosynthetic bacterium Rhodospirillum rubrum