Information on EC 5.3.1.6 - ribose-5-phosphate isomerase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
5.3.1.6
-
RECOMMENDED NAME
GeneOntology No.
ribose-5-phosphate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-Ribose 5-phosphate = D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Bifidobacterium shunt
-
Biosynthesis of antibiotics
-
Biosynthesis of secondary metabolites
-
Calvin-Benson-Bassham cycle
-
Carbon fixation in photosynthetic organisms
-
formaldehyde assimilation II (RuMP Cycle)
-
formaldehyde assimilation III (dihydroxyacetone cycle)
-
Fructose and mannose metabolism
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Pentose phosphate pathway
-
pentose phosphate pathway
BRENDA
BRENDA
BRENDA
pentose phosphate pathway (non-oxidative branch)
-
photosynthesis
BRENDA
BRENDA
BRENDA
Rubisco shunt
-
SYSTEMATIC NAME
IUBMB Comments
D-ribose-5-phosphate aldose-ketose-isomerase
Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5-phosphate ketol-isomerase
-
-
5-Phosphoribose isomerase
-
-
-
-
D-Ribose 5-phosphate isomerase
-
-
-
-
D-Ribose 5-phosphate isomerase
-
-
D-ribose-5-phosphate isomerase
-
-
D-ribose-5-phosphate isomerase
D1NPG0
-
D-ribose-5-phosphate isomerase A
-
-
D-ribose-5-phosphate isomerase B
P9WKD7
-
D-ribose-5-phosphate isomerase B
P9WKD7
-
-
D-ribose-5-phosphate ketol-isomerase
-
-
-
-
D-xylose ketol-isomerase
-
-
-
-
Isomerase, ribose phosphate
-
-
-
-
Phosphopentoisomerase
-
-
-
-
Phosphopentose isomerase
-
-
-
-
Phosphoriboisomerase
-
-
-
-
Phosphoriboisomerase
-
-
ribose 5-phosphate isomerase A
Q7MHL9
-
Ribose phosphate isomerase
-
-
-
-
Ribose-5-P isomerase
-
-
-
-
ribose-5-phosphate isomerase
A3DIL8
-
ribose-5-phosphate isomerase
A3DIL8
-
-
ribose-5-phosphate isomerase
-
-
ribose-5-phosphate isomerase
Q4CQE2
-
ribose-5-phosphate isomerase
Trypanosoma cruzi Brenner
Q4CQE2
-
-
ribose-5-phosphate isomerase B
P0CL19
-
ribose-5-phosphate isomerase B
-
-
ribose-5-phosphate isomerase B
A3DIL8
-
ribose-5-phosphate isomerase B
A3DIL8
-
-
ribose-5-phosphate isomerase type B
-
-
Ribosephosphate isomerase A
-
-
-
-
Ribosephosphate isomerase B
-
-
-
-
RPI
-
-
-
-
RPI2 protein
Q9ZU38
-
RpiA
Q8DTT9
isoform
RpiA
Q7MHL9
-
RpiB
Peptoclostridium difficile ATCC BAA-1382D-5
-
-
-
RpiB
Q8DRS5
isoform
RpiB
Q4CQE2
-
RpiB
Trypanosoma cruzi Brenner
Q4CQE2
-
-
SMU1234
Q8DTT9
isoform
SMU2142
Q8DRS5
isoform
type B ribose 5-phosphate isomerase
-
-
type B ribose 5-phosphate isomerase
Q4CQE2
-
type B ribose 5-phosphate isomerase
Trypanosoma cruzi Brenner
Q4CQE2
-
-
type B ribose-5-phosphate isomerase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-83-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene RPI2, At2g01290
UniProt
Manually annotated by BRENDA team
calf; ox
-
-
Manually annotated by BRENDA team
Chromatium sp.
strain D
-
-
Manually annotated by BRENDA team
Chromatium sp. D
strain D
-
-
Manually annotated by BRENDA team
physical interaction between phosphoribulokinase and phosphoriboisomerase in the presence of substrate
-
-
Manually annotated by BRENDA team
gene rpiB
-
-
Manually annotated by BRENDA team
strain K12, two enzyme forms: constitutive isomerase A and inducible isomerase B
-
-
Manually annotated by BRENDA team
two ribose 5-phosphate isomerases, RpiA and RpiB. RpiA is constitutively expressed, accounts for about 99% of the total ribose 5-phosphate isomerase activity for strains grown in nutrient broth. Escherichia coli strains defective in rpiA gene are still able to use ribose as a carbon source due to the presence of the second RPI, a ribose-inducible RpiB
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12, two enzyme forms: constitutive isomerase A and inducible isomerase B
-
-
Manually annotated by BRENDA team
strain DSM 2661
UniProt
Manually annotated by BRENDA team
Peptoclostridium difficile ATCC BAA-1382D-5
-
-
-
Manually annotated by BRENDA team
phosphoribulokinase and phosphoriboisomerase are associated to a complex
-
-
Manually annotated by BRENDA team
three electrophoretic forms
-
-
Manually annotated by BRENDA team
type B enzyme
UniProt
Manually annotated by BRENDA team
Trypanosoma cruzi Brenner
-
UniProt
Manually annotated by BRENDA team
strain YJ016, gene rpiA
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
Q9ZU38
deficiency in a cytosolic ribose-5-phosphate isomerase causes chloroplast dysfunction, late flowering and premature cell death in Arabidopsis thaliana
metabolism
-
ribose 5-phosphate isomerase is a key enzyme of the pentose phosphate pathway
metabolism
P9WKD7
ribose 5-phosphate isomerase is a key enzyme of the pentose phosphate pathway
metabolism
-
Rpi is involved in D-allose metabolism by converting D-ribose-5-phosphate to D-ribulose-5-phosphate and vice versa in a branch of the pentose phosphate pathway
metabolism
Q9ZU38
the cytosolic ribose-5-phosphate isomerase catalyzes the reversible interconversion of ribulose-5-phosphate and ribose-5-phosphate in the non-oxidative phase of the oxidative pentose phosphate pathway, which is part of central metabolism
metabolism
-, Q58998
two evolutionary distinct forms of the enzyme, RpiA and RpiB, with different amino acid sequences and molecular weights exist, that both catalyze the reversible conversion of ribose 5-phosphate to ribulose 5-phosphate. RpiA is found in the bacterial, plant and animal kingdoms, whereas RpiB is less widespread and is found in bacterial sources
metabolism
-
the enzyme plays an essential role in the pentose phosphate pathway and the Calvin cycle of photosynthesis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Allose
D-Psicose
show the reaction diagram
-
-
-
-
r
D-Allose
D-Psicose
show the reaction diagram
-
-
-
-
r
D-Allose
D-Psicose
show the reaction diagram
D1NPG0, -
-
-
-
r
D-Allose
D-Psicose
show the reaction diagram
-
-
-
-
r
D-Allose
D-Psicose
show the reaction diagram
-
-
-
-
?
D-Allose
D-Psicose
show the reaction diagram
-
substrates D-allose and D-psicose are preferred over ribose 5-phosphate
-
-
r
D-Allose
D-Psicose
show the reaction diagram
-
-
-
-
?
D-Allose
D-Psicose
show the reaction diagram
Peptoclostridium difficile ATCC BAA-1382D-5
-
-
-
-
r
D-allose 6-phosphate
D-allulose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-allose 6-phosphate
D-allulose 6-phosphate
show the reaction diagram
P9WKD7
-
-
-
r
D-Glucose 6-phosphate
?
show the reaction diagram
-
-
-
-
?
D-gulose
D-sorbose
show the reaction diagram
-
-
-
-
r
D-gulose
D-sorbose
show the reaction diagram
-
-
-
-
r
D-psicose
D-allose
show the reaction diagram
-
-
-
-
r
D-psicose
D-allose
show the reaction diagram
-
-
-
-
r
D-psicose
D-allose
show the reaction diagram
-
substrates D-allose and D-psicose are preferred over ribose 5-phosphate
-
-
r
D-psicose
D-allose
show the reaction diagram
A3DIL8
the conversion yield of D-psicose to D-allose is 32% for the R132E mutant enzyme and 25% for the wild type enzyme after 80 min
-
-
r
D-psicose
D-allose
show the reaction diagram
-
the enzyme convertes D-psicose to D-allose maximally at 75C and pH 8.0 with a 32% conversion yield
-
-
?
D-psicose
D-allose
show the reaction diagram
A3DIL8
the conversion yield of D-psicose to D-allose is 32% for the R132E mutant enzyme and 25% for the wild type enzyme after 80 min
-
-
r
D-psicose
D-allose
show the reaction diagram
-
the enzyme convertes D-psicose to D-allose maximally at 75C and pH 8.0 with a 32% conversion yield
-
-
?
D-Ribose
D-Ribulose
show the reaction diagram
-
-
-
-
r
D-Ribose
D-Ribulose
show the reaction diagram
-
-
-
-
r
D-Ribose
D-Ribulose
show the reaction diagram
-
-
-
-
r
D-Ribose
D-Ribulose
show the reaction diagram
-
-
-
-
?
D-Ribose
D-Ribulose
show the reaction diagram
D1NPG0, -
-
38% conversion to D-ribose 5-phosphate yield after approximately 90 min
-
r
D-Ribose
D-Ribulose
show the reaction diagram
D1NPG0, -
39% conversion yield after approximately 90 min
-
-
r
D-Ribose
D-Ribulose
show the reaction diagram
-
-
-
-
?
D-Ribose
D-Ribulose
show the reaction diagram
Peptoclostridium difficile ATCC BAA-1382D-5
-
-
-
-
r
D-ribose 5-diphosphate
D-ribulose 5-diphosphate
show the reaction diagram
P0A7Z0
-
-
?
D-ribose 5-diphosphate
D-ribulose 5-diphosphate
show the reaction diagram
Q4CQE2
-
-
-
r
D-ribose 5-diphosphate
D-ribulose 5-diphosphate
show the reaction diagram
-
substrates D-allose and D-psicose are preferred over ribose 5-phosphate
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
P0A7Z0
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
P9WKD7
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-, P9WKD7
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
O50083, -
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
D1NPG0, -
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-, Q58998
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
Q7MHL9, -
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-, P0CL19
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
Q8DRS5, Q8DTT9, -
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
diastereotopic specificity
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
D1NPG0, -
preferred substrate
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
preferred substrate
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
D1NPG0, -
preferred substrate
38% conversion to D-ribose 5-phosphate yield after approximately 90 min at 50C
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
O50083, -
direct or indirect catalytic role for the residues E107, D85 and K98
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
highest specific activity
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
enzyme is involved in the first step of the non-oxidative branch of the pentose phosphate pathway. Two ribose 5-phosphate isomerase, RpiA and RpiB. RpiA is constitutively expressed, accounts for about 99% of the total ribose 5-phosphate isomerase activity for strains grown in nutrient broth. Escherichia coli strains defective in rpiA gene are still able to use ribose as a carbon source due to the presence of the second RPI, a ribose-inducible RpiB
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
key enzyme in the oxidative and reductive pentose-phosphate pathway for the conversion of ribose-5-phosphate to ribulose-5-phosphatre and vice versa
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
P0A7Z0
the enzyme plays essential roles in carbohydrate anabolism and catabolism
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
ribose 5-phosphate ketol-isomerase, the translation product of the RKI1 gene plays a crucial role in pyridoxine synthesis in yeast
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
Q7MHL9, -
binding mode of substrate, overview
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-, Q58998
the open configuration of ribose 5-phosphate is required for isomerization and is reversibly converted to ribulose 5-phosphate
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
Chromatium sp. D
-
-
-
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
Peptoclostridium difficile ATCC BAA-1382D-5
-
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
Escherichia coli K12
-
-
-
-
D-ribose 5-triphosphate
D-ribulose 5-triphosphate
show the reaction diagram
P0A7Z0
-
-
?
D-ribose-5-phosphate
D-ribulose-5-phosphate
show the reaction diagram
Q9ZU38
-, the cytosolic ribose-5-phosphate isomerase catalyzes the reversible interconversion of ribulose-5-phosphate and ribose-5-phosphate in the non-oxidative phase of the oxidative pentose phosphate pathway
-
-
-
D-ribulose
D-ribose
show the reaction diagram
-
-
-
-
r
D-ribulose
D-ribose
show the reaction diagram
-
-
-
-
r
D-ribulose 5-diphosphate
D-ribose 5-diphosphate
show the reaction diagram
Q4CQE2
-
-
-
r
D-ribulose 5-phosphate
D-ribose 5-phosphate
show the reaction diagram
Q4CQE2
-
-
-
?
D-ribulose 5-phosphate
D-ribose 5-phosphate
show the reaction diagram
A3DIL8
-
-
-
r
D-ribulose 5-phosphate
D-ribose 5-phosphate
show the reaction diagram
Trypanosoma cruzi Brenner
Q4CQE2
-
-
-
?
D-sorbose
D-gulose
show the reaction diagram
-
-
-
-
r
D-sorbose
D-gulose
show the reaction diagram
-
lowest activity with L-sorbose
-
-
r
D-talose
D-tagatose
show the reaction diagram
D1NPG0, -
-
-
-
r
D-talose
D-tagatose
show the reaction diagram
-
-
-
-
r
L-allose
L-psicose
show the reaction diagram
D1NPG0, -
-
-
-
r
L-allose
L-psicose
show the reaction diagram
-
-
-
-
r
L-fructose
L-mannose
show the reaction diagram
-
-
-
-
r
L-fructose
L-mannose
show the reaction diagram
-
-
-
-
r
L-Lyxose
L-Xylulose
show the reaction diagram
-
-
-
-
r
L-Lyxose
L-Xylulose
show the reaction diagram
-
particularly high activity with L-lyxose
-
-
r
L-Lyxose
L-Xylulose
show the reaction diagram
Peptoclostridium difficile ATCC BAA-1382D-5
-
-
-
-
r
L-Mannose
L-Fructose
show the reaction diagram
-
-
-
-
r
L-ribose
L-ribulose
show the reaction diagram
D1NPG0, -
-
-
-
r
L-ribose
L-ribulose
show the reaction diagram
-
-
-
-
r
L-tagatose
L-talose
show the reaction diagram
-
-
-
-
r
L-tagatose
L-talose
show the reaction diagram
-
particularly high activity with L-tagatose
-
-
r
L-talose
L-tagatose
show the reaction diagram
-
-
-
-
r
L-talose
L-tagatose
show the reaction diagram
-
preferred substrate
-
-
r
L-talose
L-tagatose
show the reaction diagram
D1NPG0, -
89% conversion yield after approximately 90 min
-
-
r
L-talose
L-tagatose
show the reaction diagram
D1NPG0, -
the enzyme prefers the forward reaction, high activity, 89% conversion to L-tagatose yield after approximately 90 min at 50C
-
-
r
L-talose
L-tagatose
show the reaction diagram
-
particularly high activity with L-talose
-
-
r
L-xylulose
L-lyxose
show the reaction diagram
-
-
-
-
r
L-xylulose
L-lyxose
show the reaction diagram
-
particularly high activity with L-lyxose
-
-
r
additional information
?
-
-
the constitutive ribosephosphate isomerase A catalyzes the formation of ribose 5-phosphate from ribulose 5-phosphate and also participates in the reverse reaction during ribose and adenosine catabolism. The normal physiological role of the inducible ribosephosphate isomerase B is still uncertain
-
-
-
additional information
?
-
-
ribose 5-phosphate isomerase and ribulose-5-phosphate kinase produce and utilize, respectively, a form of ribulose 5-phosphate which is not the predominant form in the aqueous solution. The effect of this specificity will be channelling of ribulose 5-phosphate from the isomerase to the kinase during photosynthesis
-
-
-
additional information
?
-
-
physical interaction between phosphoribulokinase and ribose-5-phosphate isomerase in the presence of substrate can facilitate direct transfer of ribulose 5-phosphate between the two enzymes
-
-
-
additional information
?
-
-
the enzyme catalyzes the interconversion of D-ribose-5-phosphate and D-ribulose-5-phosphate in the reductive and oxidative pentose phosphate pathways and thus plays an important role in the primary metabolism of both photosynthetic and non-photosynthetic organisms
-
-
-
additional information
?
-
-
no substrate: D-xylose, L-rhamnose, D-altrose, D-galactose
-
-
-
additional information
?
-
-
no activity with D-allose 6-phosphate
-
-
-
additional information
?
-
-
CTRPI has a narrow substrate specificity for rare sugars and reversibly converts aldose substrates containing hydroxyl groups oriented in the same direction to one of the corresponding ketoses. CTRPI prefers aldose substrates such as L-talose, D-ribose and D-allose
-
-
-
additional information
?
-
-
enzyme substrate synthesis, overview
-
-
-
additional information
?
-
P9WKD7
enzyme substrate synthesis, overview
-
-
-
additional information
?
-
D1NPG0, -
RpiB also displays activity with L-talose, D-ribose, D-allose, L-allose, L-ribose, and D-talose in decreasing order. The enzyme shows specificity for aldose substrates possessing hydroxyl groups oriented in the same direction at the C2, C3, and C4 positions. The substrate specificity through substrate interactions with residues Tyr42, His98, and His9, which interact with the hydroxyl groups of C2, C3, and C4, respectively, oriented in the same direction, homology molecular modeling, overview
-
-
-
additional information
?
-
-
no activity is observed with D-mannose-6-phosphate
-
-
-
additional information
?
-
Q4CQE2
the enzyme cannot isomerizes D-allose 6-phosphate
-
-
-
additional information
?
-
-
enzyme displays activity only with aldose substrates possessing hydroxyl groups oriented in the right-handed configuration (Fischer projections) at the C2 and C3 positions, such as D-ribose, D-allose, L-talose, L-lyxose, D-gulose, and L-mannose. The specific activity decreases in the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
-
-
additional information
?
-
Trypanosoma cruzi Brenner
Q4CQE2
the enzyme cannot isomerizes D-allose 6-phosphate
-
-
-
additional information
?
-
Peptoclostridium difficile ATCC BAA-1382D-5
-
enzyme displays activity only with aldose substrates possessing hydroxyl groups oriented in the right-handed configuration (Fischer projections) at the C2 and C3 positions, such as D-ribose, D-allose, L-talose, L-lyxose, D-gulose, and L-mannose. The specific activity decreases in the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
-
-
additional information
?
-
-
no activity with D-allose 6-phosphate
-
-
-
additional information
?
-
Escherichia coli K12
-
the constitutive ribosephosphate isomerase A catalyzes the formation of ribose 5-phosphate from ribulose 5-phosphate and also participates in the reverse reaction during ribose and adenosine catabolism. The normal physiological role of the inducible ribosephosphate isomerase B is still uncertain
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Allose
D-Psicose
show the reaction diagram
-
-
-
-
r
D-Ribose
D-Ribulose
show the reaction diagram
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
P9WKD7
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
O50083, -
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-, Q58998
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
Q7MHL9, -
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-, P0CL19
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
Q8DRS5, Q8DTT9, -
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
D1NPG0, -
preferred substrate
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
preferred substrate
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
highest specific activity
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
enzyme is involved in the first step of the non-oxidative branch of the pentose phosphate pathway. Two ribose 5-phosphate isomerase, RpiA and RpiB. RpiA is constitutively expressed, accounts for about 99% of the total ribose 5-phosphate isomerase activity for strains grown in nutrient broth. Escherichia coli strains defective in rpiA gene are still able to use ribose as a carbon source due to the presence of the second RPI, a ribose-inducible RpiB
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
key enzyme in the oxidative and reductive pentose-phosphate pathway for the conversion of ribose-5-phosphate to ribulose-5-phosphatre and vice versa
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
P0A7Z0
the enzyme plays essential roles in carbohydrate anabolism and catabolism
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
ribose 5-phosphate ketol-isomerase, the translation product of the RKI1 gene plays a crucial role in pyridoxine synthesis in yeast
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
D-ribose-5-phosphate
D-ribulose-5-phosphate
show the reaction diagram
Q9ZU38
the cytosolic ribose-5-phosphate isomerase catalyzes the reversible interconversion of ribulose-5-phosphate and ribose-5-phosphate in the non-oxidative phase of the oxidative pentose phosphate pathway
-
-
-
D-talose
D-tagatose
show the reaction diagram
-
-
-
-
r
L-allose
L-psicose
show the reaction diagram
-
-
-
-
r
L-ribose
L-ribulose
show the reaction diagram
-
-
-
-
r
L-talose
L-tagatose
show the reaction diagram
-
preferred substrate
-
-
r
additional information
?
-
-
the constitutive ribosephosphate isomerase A catalyzes the formation of ribose 5-phosphate from ribulose 5-phosphate and also participates in the reverse reaction during ribose and adenosine catabolism. The normal physiological role of the inducible ribosephosphate isomerase B is still uncertain
-
-
-
additional information
?
-
-
ribose 5-phosphate isomerase and ribulose-5-phosphate kinase produce and utilize, respectively, a form of ribulose 5-phosphate which is not the predominant form in the aqueous solution. The effect of this specificity will be channelling of ribulose 5-phosphate from the isomerase to the kinase during photosynthesis
-
-
-
additional information
?
-
-
physical interaction between phosphoribulokinase and ribose-5-phosphate isomerase in the presence of substrate can facilitate direct transfer of ribulose 5-phosphate between the two enzymes
-
-
-
additional information
?
-
-
the enzyme catalyzes the interconversion of D-ribose-5-phosphate and D-ribulose-5-phosphate in the reductive and oxidative pentose phosphate pathways and thus plays an important role in the primary metabolism of both photosynthetic and non-photosynthetic organisms
-
-
-
additional information
?
-
-
CTRPI has a narrow substrate specificity for rare sugars and reversibly converts aldose substrates containing hydroxyl groups oriented in the same direction to one of the corresponding ketoses. CTRPI prefers aldose substrates such as L-talose, D-ribose and D-allose
-
-
-
additional information
?
-
Peptoclostridium difficile, Peptoclostridium difficile ATCC BAA-1382D-5
-
enzyme displays activity only with aldose substrates possessing hydroxyl groups oriented in the right-handed configuration (Fischer projections) at the C2 and C3 positions, such as D-ribose, D-allose, L-talose, L-lyxose, D-gulose, and L-mannose. The specific activity decreases in the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
-
-
additional information
?
-
Escherichia coli K12
-
the constitutive ribosephosphate isomerase A catalyzes the formation of ribose 5-phosphate from ribulose 5-phosphate and also participates in the reverse reaction during ribose and adenosine catabolism. The normal physiological role of the inducible ribosephosphate isomerase B is still uncertain
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
activates
Mg2+
-
activates
additional information
-
salinity shock causes decline in activity
additional information
Q4CQE2
enzyme is not metal-dependent
additional information
-
no activation by mono- or divalent cations
additional information
-
the enzyme is not activated by monovalent or divalent cations
additional information
-
1 mM Co2+, Mn2+, Mg2+, Ni2+, Zn2+, Ca2+, Cu2+, and EDTA do not influence enzyme activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-phosphoglycerate
-
-
4-deoxy-4-phosphonomethyl-D-erythronate
-
stable and potent competitive inhibitor
4-phospho-D-erythronamide
-
competitive
4-phospho-D-erythronate
-
-
4-phospho-D-erythronate
Q4CQE2
-
4-phospho-D-erythronhydrazide
Q4CQE2
-
4-phospho-D-erythronohydrazide
-
competitive
4-phospho-D-erythronohydroxamic acid
Q4CQE2
competitive
4-phosphoerythronate
-
strong competitive
4-phosphono-D-erythronate
-
-
4-phosphono-D-erythronohydroxamate
-
-
4-phosphono-D-erythronohydroxamic acid
-
competitive
5'-AMP
-
competitive
5-deoxy-5-phospho-D-ribonohydroxamate
-
-
5-deoxy-5-phospho-D-ribonohydroxamic acid
-
competitive and selective inhibitor of type B ribose-5-phosphate isomerase from Mycobacterium tuberculosis
5-deoxy-5-phospho-D-ribonohydroxamic acid
-
weak
5-phospho-D-ribonamide
P9WKD7
-
5-phospho-D-ribonate
-
competitive inhibitor of a Rpi, displays specific inhibition of Mycobacterium tuberculosis RpiB versus Escherichia coli RpiB, inhibition kinetics, overview
5-phospho-D-ribonate
-, P9WKD7
very strong competitive inhibitor of a Rpi, specific inhibition of Mycobacterium tuberculosis RpiB versus Escherichia coli RpiB, inhibition kinetics, overview
5-phospho-D-ribonohydroxamic acid
Q4CQE2
-
5-phospho-D-ribonohydroxamic acid
-
-
5-phospho-D-ribonohydroxamic acid
P9WKD7
-
6-phosphogluconate
-
competitive
6-phosphogluconate
-
temperature-dependent inhibition
6-phosphogluconate
-
noncompetitive
AMP
-
temperature-dependent inhibition
arabinose 5-phosphate
-
-
arabinose 5-phosphate
P0A7Z0
-
arabinose 5-phosphate
Q7MHL9, -
RpiA binds arabinose 5-phosphate located at the opening of the active site, the sugar ring of the inhibitor interacts with the Asp4, Lys7, Ser30, Asp118, and Lys121 residues, the phosphate group of arabinose 5-phosphate interacts with two water molecules, W51 and W82, binding mode of inhibitor, overview
D-5-Phosphoribonic acid
-
-
D-Allose 6-phosphate
-
-
D-Allose 6-phosphate
Q4CQE2
weak competitive inhibitor
D-allulose 6-phosphate
-
-
D-arabinose 5-phosphate
-
effective
D-arabinose 5-phosphate
-
-
erythrose 4-phosphate
-
competitive
fructose 6-phosphate
-
-
glyceraldehyde 3-phosphate
-
competitive
iodoacetamide
-
-
iodoacetamide
-
-
iodoacetamide
Q4CQE2
5 mM, complete inhibition
iodoacetate
-
1.25 mM, 100% loss of ribosephosphate isomerase B, no effect on ribosephosphate isomerase A
iodoacetic acid
-, P0CL19
suicide inhibitor
Mg2+
-
MgCl2, noncompetitive
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
-
-
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
P9WKD7
-
N-(5-phospho-D-ribonoyl)-glycine
-
poor inhibition with substrate D-ribose 5-phosphate, no inhibition with substrate D-allose 5-phosphate
N-(5-phospho-D-ribonoyl)-glycine
-, P9WKD7
-
N-(5-phospho-D-ribonoyl)-hydrazine
-
-
N-(5-phospho-D-ribonoyl)-hydrazine
P9WKD7
-
N-(5-phospho-D-ribonoyl)-methylamine
-
-
N-(5-phospho-D-ribonoyl)-methylamine
P9WKD7
-
Organic mercurials
-
-
-
Organic mercurials
-
-
-
Phenylmercuriacetate
-
reversible by 0.02-10 mM 2-mercaptoethanol, and by 10 mM Cys
phosphate
-
competitive
phosphate
P0A7Z0
-
ribulose diphosphate
-
1.0 mM, strong
sedoheptulose bisphosphate
-
competitive
Sodium mersalyl
-
reversible by 2-mercaptoethanol, 0.02-10 mM, and by Cys, 10 mM
Sodium salt of 2-(ethylmercurimercapto)-benzoxazole-5-carboxylic acid
-
-
Sodium salt of 2-(ethylmercurimercapto)-benzoxazole-5-carboxylic acid
-
-
sulfhydryl reagents
-
-
sulfhydryl reagents
-
-
Xylulose 5-phosphate
-
-
Mn2+
-
slight inhibition of enzyme form I and II, strong inhibition of enzyme form III
additional information
-
EDTA is not inhibitory
-
additional information
-
substrate-derived enzyme inhibitor design and synthesis of analogues of the 6-carbon high-energy intermediate postulated for the D-allose 6-phosphate to D-allulose 6-phosphate isomerization reaction, overview
-
additional information
P9WKD7
substrate-derived enzyme inhibitor design and synthesis of analogues of the 6-carbon high-energy intermediate postulated for the D-allose 6-phosphate to D-allulose 6-phosphate isomerization reaction, overview
-
additional information
-
enzyme is not affected by metal ions and not inhibited by EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
106
-
D-Allose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
460
-
D-Allose
-
pH 7.5, 40C
43
-
D-psicose
-
mutant enzyme R132E, pH 7.5, 80C
46
-
D-psicose
-
mutant enzyme R132D, pH 7.5, 80C
53
-
D-psicose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
53
-
D-psicose
-
mutant enzyme R132K, pH 7.5, 80C; wild type enzyme, pH 7.5, 80C
54
-
D-psicose
-
mutant enzyme R132Q, pH 7.5, 80C
56
-
D-psicose
-
mutant enzyme R132A, pH 7.5, 80C
64
-
D-psicose
-
at pH 8.0 and 75C
78
-
D-psicose
-
mutant enzyme R132I, pH 7.5, 80C
44
-
D-ribose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
270
-
D-ribose
-
pH 7.5, 40C
2
3
D-Ribose 5-diphosphate
Q4CQE2
muant H11A, pH 8.4, 25C
2
-
D-Ribose 5-diphosphate
Q4CQE2
mutant H102A, pH 8.4, 25C
4
-
D-Ribose 5-diphosphate
Q4CQE2
wild-type, pH 8.4, 25C
10
-
D-Ribose 5-diphosphate
Q4CQE2
mutant H138A, pH 8.4, 25C
0.017
-
D-ribose 5-phosphate
-
pH 7.5, 65C, recombinant enzyme
0.108
-
D-ribose 5-phosphate
-
-
0.16
-
D-ribose 5-phosphate
-
enzyme form III
0.17
-
D-ribose 5-phosphate
O50083, -
50C, pH 6.0, mutant enzyme D85N
0.43
-
D-ribose 5-phosphate
-
-
0.67
-
D-ribose 5-phosphate
-
enzyme form II
0.74
-
D-ribose 5-phosphate
-
-
0.77
-
D-ribose 5-phosphate
-
enzyme form I
0.83
-
D-ribose 5-phosphate
-
ribosephosphate isomerase B
0.88
-
D-ribose 5-phosphate
-
-
1
2.1
D-ribose 5-phosphate
-
at 80C and pH 7.0
1
-
D-ribose 5-phosphate
-
in 50 mM Tris-HCl, pH 7.5, at 37C
1.17
-
D-ribose 5-phosphate
O50083, -
50C, pH 6.0, wild-type enzyme
1.63
-
D-ribose 5-phosphate
-
-
1.8
-
D-ribose 5-phosphate
-
-
1.8
-
D-ribose 5-phosphate
-
-
2
-
D-ribose 5-phosphate
-
-
2.2
-
D-ribose 5-phosphate
-
-
2.39
-
D-ribose 5-phosphate
O50083, -
50C, pH 6.0, mutant enzyme D168N
2.5
-
D-ribose 5-phosphate
-
-
2.6
-
D-ribose 5-phosphate
-
calf spleen
2.7
-
D-ribose 5-phosphate
-
-
2.8
-
D-ribose 5-phosphate
-
-
3.1
-
D-ribose 5-phosphate
P0A7Z0
-
3.3
-
D-ribose 5-phosphate
-
-
3.7
-
D-ribose 5-phosphate
-
-
4.4
-
D-ribose 5-phosphate
-
ribosephosphate isomerase A
4.6
-
D-ribose 5-phosphate
-
-
5.1
-
D-ribose 5-phosphate
O50083, -
50C, pH 6.0, mutant enzyme K125A
6.5
-
D-ribose 5-phosphate
-
ox muscle
7.13
-
D-ribose 5-phosphate
O50083, -
50C, pH 6.0, mutant enzyme R100A
7.6
-
D-ribose 5-phosphate
-
at 60C and pH 7.0
9.1
10.2
D-ribose 5-phosphate
-
calf liver
17
-
D-ribose 5-phosphate
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
30
-
D-ribose 5-phosphate
-
pH 7.5, 40C
0.52
-
D-ribose-5-phosphate
-
pH 8.0, 25C, mutant enzyme D90A
0.56
-
D-ribose-5-phosphate
-
pH 8.0, 25C, mutant enzyme D87A
0.63
-
D-ribose-5-phosphate
-
pH 8.0, 25C, wild-type enzyme
1.17
-
D-ribose-5-phosphate
-
pH 8.0, 25C, mutant enzyme E91A
4.41
-
D-ribose-5-phosphate
-
pH 8.0, 25C, mutant enzyme K100A
34
-
D-ribulose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
1.4
-
D-ribulose 5-diphosphate
Q4CQE2
wild-type, pH 8.4, 25C
2.5
-
D-ribulose 5-diphosphate
Q4CQE2
mutant H102A, pH 8.4, 25C
0.015
-
D-ribulose 5-phosphate
-
pH 7.5, 65C, recombinant enzyme
0.66
-
D-ribulose 5-phosphate
-
-
5
-
D-ribulose 5-phosphate
Q4CQE2
in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30C
15
-
D-ribulose 5-phosphate
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
232
-
D-talose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
98
-
L-allose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
173
-
L-ribose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
319
-
L-ribulose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
125
-
L-tagatose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
5
20
L-talose
-
pH 7.5, 40C
37
-
L-talose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
additional information
-
additional information
O50083, -
dramatic increase of Km-value at temperatures above 80C
-
additional information
-
additional information
-
kinetics with aldose and ketose substrates, recombinant enzyme, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
200
-
D-Allose
-
pH 7.5, 40C
2682
-
D-Allose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
0.116
-
D-psicose
-
at pH 8.0 and 75C
1962
-
D-psicose
-
mutant enzyme R132K, pH 7.5, 80C
2211
-
D-psicose
-
mutant enzyme R132I, pH 7.5, 80C
2335
-
D-psicose
-
mutant enzyme R132Q, pH 7.5, 80C
2347
-
D-psicose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
2347
-
D-psicose
-
wild type enzyme, pH 7.5, 80C
2580
-
D-psicose
-
mutant enzyme R132A, pH 7.5, 80C
2674
-
D-psicose
-
mutant enzyme R132D, pH 7.5, 80C
2743
-
D-psicose
-
mutant enzyme R132E, pH 7.5, 80C
160
-
D-ribose
-
pH 7.5, 40C
11880
-
D-ribose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
1
-
D-Ribose 5-diphosphate
Q4CQE2
mutant H102A, pH 8.4, 25C
10
-
D-Ribose 5-diphosphate
Q4CQE2
mutant H138A, pH 8.4, 25C
12
-
D-Ribose 5-diphosphate
Q4CQE2
wild-type, pH 8.4, 25C
97
-
D-Ribose 5-diphosphate
Q4CQE2
muant H11A, pH 8.4, 25C
8.3
-
D-ribose 5-phosphate
O50083, -
50C, pH 6.0, mutant enzyme D85N
47
-
D-ribose 5-phosphate
-
in 50 mM Tris-HCl, pH 7.5, at 37C
120
-
D-ribose 5-phosphate
-
-
151
-
D-ribose 5-phosphate
O50083, -
50C, pH 6.0, mutant enzyme K125A
177
-
D-ribose 5-phosphate
O50083, -
50C, pH 6.0, mutant enzyme R100A
312
-
D-ribose 5-phosphate
O50083, -
50C, pH 6.0, mutant enzyme D168N
320
-
D-ribose 5-phosphate
O50083, -
50C, pH 6.0, wild-type enzyme
540
-
D-ribose 5-phosphate
-
at 60C and pH 7.0
625
-
D-ribose 5-phosphate
O50083, -
93C, pH 6, wild-type enzyme
1070
-
D-ribose 5-phosphate
-
50C, pH 7.5
1072
-
D-ribose 5-phosphate
-
50C, pH 7.5
1192
-
D-ribose 5-phosphate
-
at 80C and pH 7.0
2100
-
D-ribose 5-phosphate
P0A7Z0
-
15100
-
D-ribose 5-phosphate
-
pH 7.5, 40C
52000
-
D-ribose 5-phosphate
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C; pH 7.5, 65C, recombinant enzyme
0.0421
-
D-ribose-5-phosphate
-
pH 8.0, 25C, mutant enzyme D87A
2.5
4
D-ribose-5-phosphate
-
pH 8.0, 25C, mutant enzyme K100A
2.54
-
D-ribose-5-phosphate
-
pH 8.0, 25C, mutant enzyme K100A
13.2
-
D-ribose-5-phosphate
-
pH 8.0, 25C, mutant enzyme D90A
946
-
D-ribose-5-phosphate
-
pH 8.0, 25C, mutant enzyme E91A
3440
-
D-ribose-5-phosphate
-
pH 8.0, 25C, wild-type enzyme
9193
-
D-ribulose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
4.7
-
D-ribulose 5-diphosphate
Q4CQE2
wild-type, pH 8.4, 25C
10.7
-
D-ribulose 5-diphosphate
Q4CQE2
mutant H102A, pH 8.4, 25C
2
8
D-ribulose 5-phosphate
Q4CQE2
in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30C
50
-
D-ribulose 5-phosphate
O50083, -
50C, pH 6.0, wild-type enzyme
39530
-
D-ribulose 5-phosphate
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C; pH 7.5, 65C, recombinant enzyme
119
-
D-talose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
1506
-
L-allose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
322
-
L-ribose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
17
-
L-ribulose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
1822
-
L-tagatose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
140
-
L-talose
-
pH 7.5, 40C
13420
-
L-talose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.4
-
D-Allose
-
pH 7.5, 40C
945
0.0018
-
D-psicose
-
at pH 8.0 and 75C
2077
28
-
D-psicose
-
mutant enzyme R132I, pH 7.5, 80C
2077
37
-
D-psicose
-
mutant enzyme R132K, pH 7.5, 80C
2077
43
-
D-psicose
-
mutant enzyme R132Q, pH 7.5, 80C
2077
44
-
D-psicose
-
wild type enzyme, pH 7.5, 80C
2077
46
-
D-psicose
-
mutant enzyme R132A, pH 7.5, 80C
2077
58
-
D-psicose
-
mutant enzyme R132D, pH 7.5, 80C
2077
64
-
D-psicose
-
mutant enzyme R132E, pH 7.5, 80C
2077
0.6
-
D-ribose
-
pH 7.5, 40C
292
500
-
D-ribose 5-phosphate
-
pH 7.5, 40C
183
3029
-
D-ribose 5-phosphate
-
pH 7.5, 65C, recombinant enzyme
183
2589
-
D-ribulose 5-phosphate
-
pH 7.5, 65C, recombinant enzyme
443
0.3
-
L-talose
-
pH 7.5, 40C
6883
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.074
-
4-deoxy-4-phosphonomethyl-D-erythronate
-
25C
2.5
-
4-phospho-D-erythronamide
-
25C, pH 7.5
1.7
-
4-phospho-D-erythronate
-
-
1.8
-
4-phospho-D-erythronohydrazide
-
25C, pH 7.5
1.2
-
4-phospho-D-erythronohydroxamic acid
Q4CQE2
pH 8.4, 25C
0.028
-
4-phosphono-D-erythronate
-
25C, pH 7.5
0.057
-
4-phosphono-D-erythronohydroxamate
-
-
0.029
-
4-phosphono-D-erythronohydroxamic acid
-
25C, pH 7.5
0.4
-
5-deoxy-5-phospho-D-ribonohydroxamic acid
-
-
6.2
-
5-deoxy-5-phospho-D-ribonohydroxamic acid
-
-
0.04
-
5-phospho-D-ribonamide
-, P9WKD7
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.07
-
5-phospho-D-ribonamide
-
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.009
-
5-phospho-D-ribonate
-, P9WKD7
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.09
-
5-phospho-D-ribonohydroxamic acid
-
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.26
-
5-phospho-D-ribonohydroxamic acid
-, P9WKD7
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.43
-
5-phospho-D-ribonohydroxamic acid
-
pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate
0.7
-
arabinose 5-phosphate
-
pH 8.0, 25C
15
-
D-Allose 6-phosphate
Q4CQE2
in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30C
0.89
-
D-arabinose 5-phosphate
-
50C, pH 7.5
0.34
-
N-(5-phospho-D-ribonoyl)-glycine
-, P9WKD7
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
1.9
-
N-(5-phospho-D-ribonoyl)-hydrazine
-
pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate
0.11
-
N-(5-phospho-D-ribonoyl)-methylamine
-, P9WKD7
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.18
-
N-(5-phospho-D-ribonoyl)-methylamine
-
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
7.9
-
phosphate
-
pH 8.0, 25C
8
-
phosphate
P0A7Z0
-
4
-
Xylulose 5-phosphate
-
pH 8.0, 25C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5
-
4-phospho-D-erythronate
Q4CQE2
pH 8.4, 25C
0.7
-
4-phospho-D-erythronohydroxamic acid
Q4CQE2
pH 8.4, 25C
0.2
-
5-phospho-D-ribonamide
-
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.22
-
5-phospho-D-ribonamide
-, P9WKD7
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
1.33
-
5-phospho-D-ribonamide
-
pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate
0.031
-
5-phospho-D-ribonate
-, P9WKD7
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
1.31
-
5-phospho-D-ribonate
-
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.17
-
5-phospho-D-ribonohydroxamic acid
-
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.44
-
5-phospho-D-ribonohydroxamic acid
-, P9WKD7
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.62
-
5-phospho-D-ribonohydroxamic acid
-
pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate
2
-
D-Allose 6-phosphate
-
in 50 mM Tris-HCl, pH 7.5, at 37C
1.42
-
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
-, P9WKD7
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
1.6
-
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
-
pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate
2
-
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
-
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.57
-
N-(5-phospho-D-ribonoyl)-glycine
-, P9WKD7
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
9
-
N-(5-phospho-D-ribonoyl)-glycine
-
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
1
-
N-(5-phospho-D-ribonoyl)-hydrazine
-, P9WKD7
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.19
-
N-(5-phospho-D-ribonoyl)-methylamine
-, P9WKD7
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
0.35
-
N-(5-phospho-D-ribonoyl)-methylamine
-
pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate
0.36
-
N-(5-phospho-D-ribonoyl)-methylamine
-
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
6.3
-
D-allulose 6-phosphate
-
in 50 mM Tris-HCl, pH 7.5, at 37C
additional information
-
additional information
Q4CQE2
IC50 values of 5-phospho-D-ribonohydroxamic acid and 4-phospho-D-erythronhydrazide are above 10 mM
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0005
-
-
using D-sorbose as substrate, at 35C and pH 7.5
0.0011
-
-
using L-fructose as substrate, at 35C and pH 7.5
0.0013
-
-
using L-tagatose as substrate, at 35C and pH 7.5
0.0019
-
-
using D-allose as substrate, at 35C and pH 7.5
0.0021
-
-
using D-psicose as substrate, at 35C and pH 7.5
0.0025
-
-
using D-ribose as substrate, at 35C and pH 7.5
0.0053
-
-
using D-gulose as substrate, at 35C and pH 7.5
0.0096
-
-
using L-lyxose as substrate, at 35C and pH 7.5
0.019
-
-
using L-talose as substrate, at 35C and pH 7.5
0.027
-
-
using L-lyxose as substrate, at 35C and pH 7.5
0.048
-
-
using D-ribulose as substrate, at 35C and pH 7.5
0.058
-
-
using D-glucose 6-phosphate as substrate, at 35C and pH 7.5
0.121
-
-
using L-xylulose as substrate, at 35C and pH 7.5
0.2
-
-
after 9.1fold purification, at pH 8.0 and 75C
0.21
-
-
purified enzyme, using D-tagatose as substrate, at 65C and pH 7.5
0.259
-
-
mutant enzyme H98A, using D-psicose as substrate, pH 7.5, 80C
0.299
-
-
mutant enzyme H133A, using D-psicose as substrate, pH 7.5, 80C; mutant enzyme R136A, using D-psicose as substrate, pH 7.5, 80C
0.388
-
-
using D-ribose 5-phosphate as substrate, at 35C and pH 7.5
0.53
-
-
purified enzyme, using L-allose as substrate, at 65C and pH 7.5
0.698
-
-
mutant enzyme N99A, using D-psicose as substrate, pH 7.5, 80C
0.917
-
-
mutant enzyme T67A, using D-psicose as substrate, pH 7.5, 80C
1
-
-
substrate D-sorbose, pH 7.5, 40C
1.256
-
-
mutant enzyme H9A, using D-psicose as substrate, pH 7.5, 80C
1.815
-
-
mutant enzyme T135A, using D-psicose as substrate, pH 7.5, 80C
1.994
-
-
wild type enzyme, using D-psicose as substrate, pH 7.5, 80C
2.313
-
-
mutant enzyme R132A, using D-psicose as substrate, pH 7.5, 80C
3
-
-
substrate D-psicose, pH 7.5, 40C
7
-
-
substrate L-lyxose, pH 7.5, 40C
9
-
-
substrate L-fructose, pH 7.5, 40C
12
-
-
purified enzyme, using L-psicose as substrate, at 65C and pH 7.5
14
-
-
substrate D-ribulose, pH 7.5, 40C
15
-
-
substrate D-allose, pH 7.5, 40C
28
-
-
substrate L-talose, pH 7.5, 40C
45
-
-
substrate L-talose, pH 7.5, 40C
50
-
-
purified enzyme, using D-talose as substrate, at 65C and pH 7.5
53
-
-
substrate D-ribose, pH 7.5, 40C
57
-
-
substrate L-xylulose, pH 7.5, 40C
120
-
-
substrate D-gulose, pH 7.5, 40C
187
-
-
cell lysate, at 50C and pH 7.0
272
-
-
purified enzyme, using L-ribose as substrate, at 65C and pH 7.5
290
-
-
after purification, at 50C and pH 7.0
600
-
-
purified enzyme, using L-allose as substrate, at 65C and pH 7.5
720
-
-
purified enzyme, using L-ribulose as substrate, at 65C and pH 7.5
1037
-
-
purified enzyme, using D-psicose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-psicose
1352
-
-
purified enzyme, using D-allose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-allose
1700
-
-
-
5374
-
-
purified enzyme, using D-ribulose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-ribulose
5800
-
-
purified enzyme, using D-ribose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-ribose
7363
-
-
purified enzyme, using L-talose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate L-talose
19680
-
-
purified enzyme, using D-ribulose 5-phosphate as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-ribulose 5-phosphate
25690
-
-
purified enzyme, using D-ribose 5-phosphate as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-ribose 5-phosphate
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
O50083, -
at 50C
7
9
-
-
7.4
-
Q9ZU38
assay at
7.5
-
-
optimum for synthesis of D-allose
7.5
-
P9WKD7
assay at
7.7
7.8
-
D-ribulose 5-phosphate, D-ribose 5-phosphate
8
10
Q4CQE2
broad
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
more than 80% of its maximal activity is maintained at pH values from 6.0 to 9.0
6
9.9
-
pH 6: about 40% of maximal activity, pH 9.9: about 65% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
P9WKD7
assay at
37
-
Q9ZU38
assay at
65
-
-
-
65
-
-
optimum for synthesis of D-allose
85
-
-
-
95
-
O50083, -
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
80
-
30C: about 50% of maximal activity, 80C: about 45% of maximal activity
40
99
-
enzyme activity increases significantly when the temperature increases until 80C. The optimum temperature is 80C. The activity at 30C is 25% of that at 80C. The enzyme activity decreases after 80C. It is still highly active when the temperature reaches 99C, 90% activity of that of 80C. This enzyme shows relatively high activity (above 50% of its maximum activity) over a large temperature range of 40-99C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.77
-
Q7MHL9, -
isoelectric focusing
5.1
-
-
isoelectric focusing
6.4
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
one electrophorectic form
Manually annotated by BRENDA team
-
two electrophorectic forms
Manually annotated by BRENDA team
Q4CQE2
highest expression
Manually annotated by BRENDA team
-
two electrophorectic forms
Manually annotated by BRENDA team
-
one electrophorectic form
Manually annotated by BRENDA team
-
one electrophorectic form
Manually annotated by BRENDA team
-
one electrophorectic form
Manually annotated by BRENDA team
-
two electrophorectic forms
Manually annotated by BRENDA team
-
two electrophorectic forms
Manually annotated by BRENDA team
-
two electrophoretic forms
Manually annotated by BRENDA team
Q4CQE2
metacyclic and in cell-culture
Manually annotated by BRENDA team
-
two electrophorectic forms
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
co-localization of enzyme with phosphoribulokinase and Rubisco
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Anaplasma phagocytophilum (strain HZ)
Bartonella henselae (strain ATCC 49882 / Houston 1)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain WY96-3418)
Giardia intestinalis (strain ATCC 50803 / WB clone C6)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Lactobacillus salivarius (strain UCC118)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Vibrio vulnificus (strain YJ016)
Vibrio vulnificus (strain YJ016)
Vibrio vulnificus (strain YJ016)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30000
35000
-
gel filtration
32000
34000
-
ribosephosphate isomerase B, gel filtration
32000
-
-
dynamic light scattering
34000
-
-
non-denaturing PAGE
34000
-
-
gel filtration
34000
-
-
gel filtration
35000
-
-
about, native PAGE, recombinant enzyme
35200
-
-
gel filtration
39600
-
Q4CQE2
gel filtration
45000
-
-
ribosephosphate isomerase A, gel filtration
45000
-
Q7MHL9, -
recombinant detagged RpiA, dynamic light scattering and gel filtration
49000
-
-
gel filtration
50000
-
-
dynamic light scattering
53000
-
-
high-speed equilibrium centrifugation
54000
-
Chromatium sp.
-
-
57000
-
-
gel filtration
96000
-
-
gel filtration
98000
-
O50083, -
gel filtration
105000
-
-
gel filtration
183000
-
-
gel filtration
228000
-
-
analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 16000, SDS-PAGE
?
-
x * 25300, SDS-PAGE
?
-
x * 26400, SDS-PAGE
?
-
x * 15867, calculated from amino acid sequence
?
Q8DRS5, Q8DTT9, -
x * 23400, isoform RpiB, calculated from amino acid sequence
?
Q8DRS5, Q8DTT9, -
x * 24570, isoform RpiA, calculated from amino acid sequence
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 25000, SDS-PAGE
dimer
-
2 * 17300, calculation from nucleotide sequence
dimer
-
2 * 25066, calculation from nucleotide sequence
dimer
P0A7Z0
the two subunits in the dimer have different conformations, the result of motion of two largely rigid domains with respect to each other in the subunit
dimer
Q4CQE2
2 * 17400, calculated, 2 * 18000, SDS-PAGE
dimer
Q7MHL9, -
2 * 20000-25000, RpiA
dimer
-
2 x 17500, about, recombinant enzyme, RpiB has an active-site interface between the dimer structures
dimer
-
2 * 17217, calculated, 2 * 17200, SD-PAGE
dimer
Peptoclostridium difficile ATCC BAA-1382D-5
-
2 * 17217, calculated, 2 * 17200, SD-PAGE
-
homodimer
-
2 * 16800, SDS-PAGE
homodimer
-
2 * 17000, gel filtration
homodimer
-
2 * 17000, X-ray crystallography
homodimer
-
2 * 16015, calculated from amino acid sequence
homodimer
-
2 * 17000, X-ray crystallography
-
homodimer
-
2 * 16800, SDS-PAGE, 2 * 16015, calculated from amino acid sequence
-
tetramer
-
4 * 58000, SDS-PAGE
tetramer
-
4 * 26000, SDS-PAGE
tetramer
Q4CQE2
x-ray crystallography
tetramer
O50083, -
4 * 25163, calculation from nucleotide sequence
tetramer
O50083, -
4 * 26000, in crystal and in solution, each monomer has a new fold consisting of two alpha/beta domains, SDS-PAGE
tetramer
-, Q58998
RpiA crystal structure, overview
tetramer
Trypanosoma cruzi Brenner
-
x-ray crystallography
-
trimer
-
1 * 75000, alpha, + 2 * 54000, beta, SDS-PAGE
homotetramer
-
4 * 24000, SDS-PAGE, 4 * 23724, calculated from amino acid sequence
additional information
-
homology modeling of RpiB, substrate binding structure, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
co-crystallization in the presence of 20 mM ribose-5-phosphate or 20 mM ribose-5-phosphate with 12 mM MnCl2, sitting drop vapor diffusion method, using 0.1 M Na citrate pH 5.0, 20% (w/v) PEG 6000
-, P0CL19
hanging drop vapor diffusion method, enzyme form RpiA
-
hanging drop vapor diffusion method, structure of a complex with arabinose 5-phosphate at 1.25 A resolution
P0A7Z0
purified recombinant MJ1603, microbatch-under-oil method, 0.0005 ml of 8.1 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, containing 200 mM NaCl are mixed with 0.0005 ml of crystallization reagent, consisting of 0.1 M acetate, pH 4.5 containing 40% v/v 1,2-propanediol and 0.05 M calcium acetate, 18C. The mixture is covered with 0.015 ml silicone and paraffin oil, X-ray diffraction structure determination and analysis at 1.78 A resolution, molecular replacement and modeling
-, Q58998
hanging drop vapour diffusion method, X-ray structure of ribose-5-phosphate isomerase B in complex with the inhibitors 4-phosphono-D-erythronohydroxamate and 4-phospho-D-erythronate refined to resolutions of 2.1 and 2.2 A
-
in complex with 5-deoxy-5-phospho-D-ribonohydroxamate, hanging drop vapour diffusion method, with 15% PEG 8000, 0.1 M MES buffer, pH 6, 5% PEG 1000, and 0.2 M Li2SO4, or in complex with D-ribose 5-phosphate, sitting drop vapour diffusion method, with 20% PEG 3K, 0.1 M Tris, pH 7, and 0.2 M Ca acetate
-
sitting drop vapour diffusion method
-
molecular dockng using L-xylose and D-ribose as the substrate. Residue M95 seems to be a determinant residue for the specificity on free sugars
-
molecular replacement at 2.9 A resolution
-
hanging drop vapor diffusion method, crystal structure of the free enzyme and the complex with D-4-phosphoerythronic acid
O50083, -
in complex with ribose 5-phosphate, ribose or allose, sitting drop vapor diffusion method, using 0.05 M Tris pH 7.0, 10% (w/v) PEG 8000, 0.15 M magnesium chloride, and 0.2 M potassium chloride
-
purified recombinant RpiB, sitting drop vapour diffusion method, 0.001 ml of 7 mg/ml protein in mM Tris-HCl buffer pH 7.5 is mixed with 0.001 ml of reservoir solution, containing 0.05 M Tris, pH 7.0, 10% PEG 8000, 0.15 M MgCl2 and 0.2 M KCl, and equilibrated against 1 ml of reservoir solution, 3 weeks, flash-cooling in liquid nitrogen with a cryoprotectant solution containing 65 mM Tris pH 7.0, 13% PEG 8000, 195 mM MgCl2, 260 mM KCl and 20% glycerol, X-ray diffraction structure determination and analysis at 1.9 A resolution, modeling
-
2.1 A resolution crystal structure. Crystals are cryo-protected by transfering through crystallization solution with progressively higher ethylene glycol concentration up to 30% v/v and then flash cooled in liquid nitrogen. The protein crystallizes in space group F432 with cell dimensions a = b = c = 209A, corresponding to one molecule per asymmetric unit and a solvent content of 47%
-
sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M ammonium acetate, 0.1 M HEPES pH 7.5, 0.1 M NaCl, 2.0 M ammonium sulfate; sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M ammonium acetate, 0.1 M Tris-HCl pH 8.5 and 25% (w/v) PEG 3350, 0.2 M MgCl2, 0.1 M Tris-HCl pH 8.5
Q8DRS5, Q8DTT9, -
crystal structure of enzyme complexed with the open chain form of the ribose 5-phosphate and the open chain form of the C2 epimeric inhibitor arabinose 5-phosphate as well as the apo form at high resolution
-
RpiB (wild type or C69A mutant enzyme), sitting drop vapor diffusion method, using 0.5% (v/v) Jeffamine ED-2001, 0.1 M HEPES, 1.1 M Na-malonate (pH 7.0) for the wild type enzyme in complex with phosphate, or 0.8 M Na?K phosphate (pH 8.2) for the mutant enzyme C69A in complex with phosphate, or 20% (w/v) poly(ethyleneglycol) 550 monomethyl ether, 0.1 M NaCl, 0.1 M bicine (pH 9.0) for the wild type enzyme in complex with D-ribose 5-phosphate, or 20% (w/v) poly(ethylene glycol) 6000, 0.2 M ammonium chloride, 0.1 M Tris-HCl (pH 8.0) for wild type enzyme in complex with 4-phospho-D-erythronohydroxamic acid, or 20% (w/v) poly(ethylene glycol) 3350, 0.2 M sodium acetate, 0.1 M bis-Tris propane (pH 8.5) for mutant enzyme C69A in complex with allose 6-phosphate
Q4CQE2
open form RpiA in complex with substrate ribose 5-phosphate, the closed form complexed with arabinose-5-phosphate, and the apo-RpiA, hanging drop vapor diffusion method, 0.002 ml of 30 mg/ml protein in 20 mM HEPES, pH 7.5, and 150 mM KCl are mixed with 0.002 ml of a reservoir solution containing 50 mM succinate, pH 4.1, 180 mM ammonium sulfate, and 8% PEG 4000, 3 days, 20C, for complexed enzyme addition of 20 mM ligand, X-ray diffraction structure determination and analysis at 1.49-2.07 A resolution, molecular replacement
Q7MHL9, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
10
-
65C, stable for at least 30 min
5
10
-
45C, stable for at least 30 min
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
50
-
enzyme activity is stable for 48 h at 35C, and shows half-lives of 15 h at 40C, and 6 h at 50C
45
-
-
30 min, ribosephosphate isomerase A retains 90% of its activity, ribosephosphate isomerase B retains 60% of its activity
45
-
-
pH 5-10, stable for at least 30 min
50
-
-
half-life 96 h
55
-
-
half-life 53 min
57
-
-
1 h, 50% loss of activity
60
75
-
the half-lives of the wild type enzyme at 60C, 65C, 70C, 75C, and 80C are 11, 7.0, 4.2, 1.5, and 0.6 h, respectively
60
80
-
the purified enzyme at 0.1 mg/ml is very stable at 60 and 70C but is deactivated at 80C. The enzyme shows half lifetimes of 70.8, 53.1, 6.4, and 1.2 h at 60, 70, 80, and 90C, respectively
60
-
-
ribosephosphate isomerase A: complex dependence on protein concentration, at 1.0 mg/ml protein and greater, all activity is lost. At 0.05-0.75 mg/ml protein, 20-30% of the original activity is left after 30 min; ribosephosphate isomerase B: half-life 2.2 min, independent of enzyme and protein concentration
65
-
-
pH 5-10, stable for at least 30 min
65
-
-
half-life 4.7 h
75
-
-
the half-life at 75C is 3.3 h
91
-
-
1 h, 50% loss of activity
100
-
O50083, -
stability and integrity up to, needs at least 250 mM NaCl to maintain its hyperthermostability
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(NH4)2SO4, NaCl, KCl and LiCl increase thermal stability. LiBr, CaCl2, methanol, ethanol, and 1-propanol decrease thermal stability. Alcohols decrease the stability in the following order: methanol, ethanol, propanol
-
ethylene glycol increases stability
-
freezing and thawing destroys activity
-
maximum activities in sodium dihydrogen phosphate-ciitric acid buffer at pH 6.5-8.0 and in 50 mM Tris-HCl buffer pH 7.0-9.0. This enzyme retains about 65% activity from pH 8.8-11.0 in glycine-NaOH buffer
-
(NH4)2SO4, NaCl, KCl and LiCl increase thermal stability. LiBr, CaCl2, methanol, ethanol, and 1-propanol decrease thermal stability. Alcohols decrease the stability in the following order: methanol, ethanol, propanol
-
ethylene glycol has little effect on the mesophilic enzyme
-
freeze-labile
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, stable for 2 weeks
-
-20C, stable for several months
-
-20C, stable for several weeks
-
2C, stable for several months
-
4C, stable for several months
-
-20C, 2 months, stable
-
4C, stable for 6-8 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ox muscle, calf spleen and liver, partial
-
Ni-NTA column chromatography and Superdex 75 gel filtration
-, P0CL19
3 forms: I, I, III
-
affinity chromatographic method
-
recombinant MJ1603 from Escherichia coli strain Rosetta (DE3) by anion exchange and hydroxyapatite chromatography, and gel filtration
-, Q58998
HisTrap HP column chromatography
-
HisTrap HP column chromatography; recombinant RpiB from Escherichia coli strain ER2566 by His affinity chromatography
-
recombinant RpiB from Escherichia coli strain ER2566 by His affinity chromatography
-
recombinant enzyme
-
Ni2+-chelating column chromatography and Superdex S75 gel filtration; Ni2+-chelating column chromatography and Superdex S75 gel filtration
Q8DRS5, Q8DTT9, -
HiTrap Q anion exchange column chromatography and Sephacryl S-300 gel filtration
-
Ni-affinity column chromatography
-
heat precipitation
-
Superdex 75 gel filtration
Q4CQE2
recombinant His-tagged RpiA from Escherichia coli strain BL21(DE3) by nickel affinity chromatography. The His-tag is cleaved off and removed, folowed by anion exchange chromatography and gel filtration
Q7MHL9, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene RPI2, phylogenetic analysis
Q9ZU38
expressed in Escherichia coli BL21 (DE3) R3 Rosetta cells
-, P0CL19
overexpression as a His-tagged Se-Met-labeled protein
P0A7Z0
expression of MJ1603 in Escherichia coli strain Rosetta (DE3)
-, Q58998
expressed in Escherichia coli Top10 cells
-
overexpression in Escherichia coli
-
expression in Escherichia coli
-
overexpression in Escherichia coli
O50083, -
expressed in Escherichia coli ER2566 cells
-
expressed in Escherichia coli ER2566 cells; gene rpiB, expression in Escherichia coli strain ER2566
-
expression in Escherichia coli
-
gene rpiB, expression in Escherichia coli strain ER2566
-
overexpression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
Q8DRS5, Q8DTT9, -
expressed in Escherichia coli ER2566 cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli ER2566 cells
Q4CQE2
gene rpiA, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
Q7MHL9, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C65A
-
the mutant shows no activity for D-psicose
D8A
-
the mutant shows no activity for D-psicose
H133A
-
the mutant shows 15% activity compared to the wild type enzyme
H98A
-
the mutant shows 13% activity compared to the wild type enzyme
H9A
-
the mutant shows 63% activity compared to the wild type enzyme
N99A
-
the mutant shows 35% activity compared to the wild type enzyme
R132A
-
the mutant exhibits an increase in D-psicose isomerization activity (116% activity compared to the wild type enzyme)
R132D
-
the mutant shows increased catalytic efficiency toward D-psicose compared to the wild type enzyme
R132E
-
the mutant shows increased catalytic efficiency toward D-psicose compared to the wild type enzyme, the specific activity and catalytic efficiency (kcat/Km) of the R132E mutant for D-psicose are 1.4 and 1.5fold higher than those of the wild type enzyme, respectively
R132I
-
the mutant shows decreased catalytic efficiency toward D-psicose compared to the wild type enzyme
R132K
-
the mutant shows decreased catalytic efficiency toward D-psicose compared to the wild type enzyme
R132Q
-
the mutant shows decreased catalytic efficiency toward D-psicose compared to the wild type enzyme
R136A
-
the mutant shows 15% activity compared to the wild type enzyme
T135A
-
the mutant shows 91% activity compared to the wild type enzyme
T67A
-
the mutant shows 46% activity compared to the wild type enzyme
Y42A
-
the mutant shows no activity for D-psicose
C65A
-
the mutant shows no activity for D-psicose
-
H9A
-
the mutant shows 63% activity compared to the wild type enzyme
-
N99A
-
the mutant shows 35% activity compared to the wild type enzyme
-
R136A
-
the mutant shows 15% activity compared to the wild type enzyme
-
T135A
-
the mutant shows 91% activity compared to the wild type enzyme
-
R189K
-
6% of the wild-type activity. Loss of the structural integrity of the protein seems to be responsible for the greatly diminished activity
D87A
-
turnover number with D-ribose-5-phosphate is 0.0012% of value for the the wild-type enzyme, moderate change in Km-value
D90A
-
turnover number with D-ribose-5-phosphate is 0.38% of value for the the wild-type enzyme, moderate change in Km-value
E91A
-
turnover number with D-ribose-5-phosphate is 27.5% of value for the the wild-type enzyme, moderate change in Km-value
K100A
-
turnover number with D-ribose-5-phosphate is 0.074% of value for the the wild-type enzyme, moderate change in Km-value
C69A
Q4CQE2
inactive
C69A
Q4CQE2
no catalytic activity
H102A
Q4CQE2
kinetics severeyl impaired with substrate ribose 5-phosphate, but not affected with substrate ribulose 5-phosphate
H11A
Q4CQE2
6fold increase in Km value, 8fold increase in kcat value, decrease in stability to freezing and thawing
H138A
Q4CQE2
little variations in kinetics compared to wild-type
C69A
Trypanosoma cruzi Brenner
-
inactive
-
additional information
Q9ZU38
construction of T-DNA knockout mutants of the RPI2 gene, which encodes the cytosolic ribose-5-phosphate isomerase. Knockout of the RPI2 gene does not significantly change the total RPI activity in the mutant plants, but knockout of RPI2 interferes with chloroplast structure and decreases chloroplast photosynthetic capacity. Rpi2 mutants accumulate less starch in the leaves and flower significantly later than wild-type when grown under short-day conditions, and rpi2 mutants display premature cell death in the leaves when grown at an above-normal temperature of 26C, phenotypes, detailed overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
production of D-allose from D-psicose by enzyme. At pH 7.5 and 50C, synthesis of 165 g D-allose per l within 6 h
synthesis
-
RpiB is a potential producer of L-form monosaccharides