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5.3.1.29: ribose 1,5-bisphosphate isomerase

This is an abbreviated version!
For detailed information about ribose 1,5-bisphosphate isomerase, go to the full flat file.

Word Map on EC 5.3.1.29

Reaction

alpha-D-ribose 1,5-bisphosphate
=
D-ribulose 1,5-bisphosphate

Synonyms

PH0208, R15P isomerase, R15Pi, ribulose 1,5-bisphosphate synthase, RuBP synthase, Tk-E2b2

ECTree

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.1 Interconverting aldoses and ketoses, and related compounds
                5.3.1.29 ribose 1,5-bisphosphate isomerase

Engineering

Engineering on EC 5.3.1.29 - ribose 1,5-bisphosphate isomerase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C135S
mutation of catalytic residue, inhibits binding of substrate ribose 1,5-bisphosphate. Mutation does not not alter the binding behavior of AMP to the protein
D204N
mutation of catalytic residue. Mutation does not not alter the binding behavior of AMP to the protein
C135S
-
mutation of catalytic residue, inhibits binding of substrate ribose 1,5-bisphosphate. Mutation does not not alter the binding behavior of AMP to the protein
-
D204N
-
mutation of catalytic residue. Mutation does not not alter the binding behavior of AMP to the protein
-
C133A
inactive mutant enzyme
C133S
inactive mutant enzyme
D202N
inactive mutant enzyme
R227R
mutant enzyme exhibits a decrease in molecular size of the enzyme and significantly decreases the enzymatic activity