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Information on EC 5.3.1.6 - ribose-5-phosphate isomerase
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5.3.1.6 ribose-5-phosphate isomeraseIUBMB Comments
Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
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Word Map
- 5.3.1.6
-
indentation
- ribulose-5-phosphate
- clasp
- transaldolase
-
denture
- d-allose
- phosphoribulokinase
-
calvin
-
3-epimerase
- d-psicose
- peri-implantitis
- rri
- synthesis
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
rpi, ribose-5-phosphate isomerase, phosphoriboisomerase, ribose phosphate isomerase, ctrpi, d-ribose-5-phosphate isomerase, ribosephosphate isomerase b, ribosephosphate isomerase a, ribose 5-phosphate isomerase a, ribose-5-phosphate isomerase b, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CTRpiB
D-Ribose 5-phosphate isomerase
D-ribose-5-phosphate isomerase B
MtRpiB
Phosphoriboisomerase
ribose-5-phosphate isomerase
ribose-5-phosphate isomerase B
RPI
RpiA
RpiB
Tc00.1047053509199.24
TM1080
type B ribose 5-phosphate isomerase
type B ribose-5-phosphate isomerase
type B Rpi
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-Ribose 5-phosphate = D-ribulose 5-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
D-ribose-5-phosphate aldose-ketose-isomerase
Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
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CAS REGISTRY NUMBER
COMMENTARY
9023-83-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-Allose
D-Psicose
AM180355
the specific activity follows the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
?
D-Allose
D-Psicose
AM180355
the specific activity follows the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
?
D-Allose
D-Psicose
-
substrates D-allose and D-psicose are preferred over ribose 5-phosphate
-
r
D-Allose
D-Psicose
the specific activity follows the order L-talose, D-ribose, D-allose, L-allose, L-lyxose, L-ribose, D-tallose
-
?
D-Allose
D-Psicose
the specific activity follows the order L-talose, D-ribose, D-allose, L-allose, L-lyxose, L-ribose, D-tallose
-
?
D-gulose
D-sorbose
AM180355
the specific activity follows the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
?
D-psicose
D-allose
-
substrates D-allose and D-psicose are preferred over ribose 5-phosphate
-
r
D-psicose
D-allose
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
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
-
the enzyme convertes D-psicose to D-allose maximally at 75°C and pH 8.0 with a 32% conversion yield
-
?
D-psicose
D-allose
-
the enzyme convertes D-psicose to D-allose maximally at 75°C and pH 8.0 with a 32% conversion yield
-
?
D-Ribose
D-Ribulose
AM180355
the specific activity follows the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
?
D-Ribose
D-Ribulose
AM180355
the specific activity follows the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
?
D-Ribose
D-Ribulose
A0A4S5F2E5
-
38% conversion to D-ribose 5-phosphate yield after approximately 90 min
r
D-Ribose
D-Ribulose
A0A4S5F2E5
39% conversion yield after approximately 90 min
-
r
D-Ribose
D-Ribulose
the specific activity follows the order L-talose, D-ribose, D-allose, L-allose, L-lyxose, L-ribose, D-tallose
-
?
D-Ribose
D-Ribulose
the specific activity follows the order L-talose, D-ribose, D-allose, L-allose, L-lyxose, L-ribose, D-tallose
-
?
D-ribose 5-diphosphate
D-ribulose 5-diphosphate
-
substrates D-allose and D-psicose are preferred over ribose 5-phosphate
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
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
the enzyme plays essential roles in carbohydrate anabolism and catabolism
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
A0A4S5F2E5
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
A0A4S5F2E5
preferred substrate
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
preferred substrate
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
A0A4S5F2E5
preferred substrate
38% conversion to D-ribose 5-phosphate yield after approximately 90 min at 50°C
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
direct or indirect catalytic role for the residues E107, D85 and K98
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
diastereotopic specificity
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
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
-
highest specific activity
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
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
binding mode of substrate, overview
-
r
D-ribose-5-phosphate
D-ribulose-5-phosphate
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 5-phosphate
D-ribose 5-phosphate
-
-
r
D-talose
D-tagatose
the specific activity follows the order L-talose, D-ribose, D-allose, L-allose, L-lyxose, L-ribose, D-tallose
-
?
L-allose
L-psicose
the specific activity follows the order L-talose, D-ribose, D-allose, L-allose, L-lyxose, L-ribose, D-tallose
-
?
L-Lyxose
L-Xylulose
AM180355
the specific activity follows the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
?
L-Lyxose
L-Xylulose
AM180355
the specific activity follows the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
?
L-Lyxose
L-Xylulose
-
particularly high activity with L-lyxose
-
r
L-Lyxose
L-Xylulose
the specific activity follows the order L-talose, D-ribose, D-allose, L-allose, L-lyxose, L-ribose, D-tallose
-
?
L-Lyxose
L-Xylulose
the specific activity follows the order L-talose, D-ribose, D-allose, L-allose, L-lyxose, L-ribose, D-tallose
-
?
L-Mannose
L-Fructose
AM180355
the specific activity follows the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
?
L-Mannose
L-Fructose
AM180355
the specific activity follows the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
?
L-ribose
L-ribulose
the specific activity follows the order L-talose, D-ribose, D-allose, L-allose, L-lyxose, L-ribose, D-tallose
-
?
L-tagatose
L-talose
-
particularly high activity with L-tagatose
-
r
L-talose
L-tagatose
AM180355
the specific activity follows the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
?
L-talose
L-tagatose
A0A4S5F2E5
89% conversion yield after approximately 90 min
-
r
L-talose
L-tagatose
A0A4S5F2E5
the enzyme prefers the forward reaction, high activity, 89% conversion to L-tagatose yield after approximately 90 min at 50°C
-
r
L-talose
L-tagatose
-
particularly high activity with L-talose
-
r
L-talose
L-tagatose
the specific activity follows the order L-talose, D-ribose, D-allose, L-allose, L-lyxose, L-ribose, D-tallose
-
?
L-xylulose
L-lyxose
-
particularly high activity with L-lyxose
-
r
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
?
-
AM180355
the 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
-
?
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
?
-
AM180355
the 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
-
?
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 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
?
-
-
no substrate: D-xylose, L-rhamnose, D-altrose, D-galactose
-
?
additional information
?
-
A0A4S5F2E5
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
?
-
-
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
?
-
-
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
?
-
A0A4S5F2E5
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
?
-
enzyme exhibits activity with D-form of various aldose substrates in the order of D-ribose > D-talose > D-allose > D-arabinose
-
?
additional information
?
-
-
enzyme exhibits activity with D-form of various aldose substrates in the order of D-ribose > D-talose > D-allose > D-arabinose
-
?
additional information
?
-
no activity with D-allose 6-phosphate
-
?
additional information
?
-
-
no activity with D-allose 6-phosphate
-
?
additional information
?
-
enzyme substrate synthesis, overview
-
?
additional information
?
-
-
enzyme substrate synthesis, overview
-
?
additional information
?
-
no activity with D-allose 6-phosphate
-
?
additional information
?
-
enzyme substrate synthesis, overview
-
?
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 activity is observed with D-mannose-6-phosphate
-
?
additional information
?
-
the enzyme displays activity only with aldose substrates having hydroxyl groups configured in the same direction at the C2, C3, and C4 positions
-
?
additional information
?
-
the enzyme displays activity only with aldose substrates having hydroxyl groups configured in the same direction at the C2, C3, and C4 positions
-
?
additional information
?
-
the enzyme cannot isomerizes D-allose 6-phosphate
-
?
additional information
?
-
-
the enzyme cannot isomerizes D-allose 6-phosphate
-
?
additional information
?
-
the enzyme cannot isomerizes D-allose 6-phosphate
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-ribose-5-phosphate
D-ribulose-5-phosphate
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-ribose 5-phosphate
D-ribulose 5-phosphate
-
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
the enzyme plays essential roles in carbohydrate anabolism and catabolism
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
A0A4S5F2E5
preferred substrate
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
preferred substrate
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
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
-
highest specific activity
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
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
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
?
-
-
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
?
-
-
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 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
?
-
A0A4S5F2E5
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
?
-
-
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
?
-
-
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
no activation by mono- or divalent cations
additional information
-
1 mM Co2+, Mn2+, Mg2+, Ni2+, Zn2+, Ca2+, Cu2+, and EDTA do not influence enzyme activity
additional information
-
the enzyme is not activated by monovalent or divalent cations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3S)-3-hydroxy-1-(6-oxo-1,4,5,6-tetrahydropyridazine-3-carbonyl)pyrrolidine-2-carboxylic acid
inhibitor identified by in silico analysis, shows best docking score of -12.735 forming six hydrogen bonds and one salt bridge
4-deoxy-4-phosphonomethyl-D-erythronate
-
stable and potent competitive inhibitor
Mn2+
-
slight inhibition of enzyme form I and II, strong inhibition of enzyme form III
[(2R,3S,4R,5R,6S)-3,4,5,6-tetrahydroxyoxan-2-yl]methyl hydrogen sulfate
inhibitor identified by in silico analysis, second best hit with dock-ing score of -11.927 and is predict to make eight hydrogenbonds, two electrostatic interactions and one possible pi-pi interaction
5-deoxy-5-phospho-D-ribonohydroxamic acid
-
competitive and selective inhibitor of type B ribose-5-phosphate isomerase from Mycobacterium tuberculosis
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
very strong competitive inhibitor of a Rpi, specific inhibition of Mycobacterium tuberculosis RpiB versus Escherichia coli RpiB, inhibition kinetics, overview
arabinose 5-phosphate
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
iodoacetate
-
1.25 mM, 100% loss of ribosephosphate isomerase B, no effect on ribosephosphate isomerase A
N-(5-phospho-D-ribonoyl)-glycine
-
poor inhibition with substrate D-ribose 5-phosphate, no inhibition with substrate D-allose 5-phosphate
Phenylmercuriacetate
-
reversible by 0.02-10 mM 2-mercaptoethanol, and by 10 mM Cys
Phenylmercuriacetate
-
reversible by 0.02-10 mM 2-mercaptoethanol, and by 10 mM Cys
Sodium mersalyl
-
reversible by 2-mercaptoethanol, 0.02-10 mM, and by Cys, 10 mM
Sodium mersalyl
-
reversible by 2-mercaptoethanol, 0.02-10 mM, and by Cys, 10 mM
Sodium salt of 2-(ethylmercurimercapto)-benzoxazole-5-carboxylic acid
-
-
additional information
-
enzyme is not affected by metal ions and not inhibited by EDTA
-
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
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
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acromegaly
Hypertension is Common in Patients with Newly Diagnosed Acromegaly and is Independently Associated with Renal Resistive Index.
Adenoma
Is intravenous urography mandatory in the management of benign prostatic hyperplasia?
Amblyopia
Retinitis pigmentosa inversa with unilateral high myopia with fellow eye optic disc pitting.
Anemia
Clinical significance of immature reticulocyte fraction determined by automated reticulocyte counting.
Anemia, Iron-Deficiency
Clinical significance of immature reticulocyte fraction determined by automated reticulocyte counting.
Apnea
Screening for Obstructive Sleep Apnea in Commercial Drivers Using EKG-Derived Respiratory Power Index.
Atherosclerosis
Dietary rice protein isolate attenuates atherosclerosis in apoE-deficient mice by upregulating antioxidant enzymes.
Autoimmune Diseases
Anti-RNA polymerase I antibodies in the sera of MRL lupus mice at the initial stages of disease are directed primarily against phosphorylation-dependent epitopes.
Bacterial Infections
Retrograde Peri-Implantitis: A Case Report Introducing An Approach to its Management.
Bone Diseases
Site-Dependent Reference Point Microindentation Complements Clinical Measures for Improved Fracture Risk Assessment at the Human Femoral Neck.
Bone Diseases
The inferomedial femoral neck is compromised by age but not disease: Fracture toughness and the multifactorial mechanisms comprising reference point microindentation.
Brain Neoplasms
Assessment of Vascular Supply of Hypervascular Extra-Axial Brain Tumors with 3T MR Regional Perfusion Imaging.
Breast Neoplasms
In vitro actions on human cancer cells and the liquid chromatography-mass spectrometry/mass spectrometry fingerprint of phytochemicals in rice protein isolate.
Carcinogenesis
A rice protein isolate alters 7,12-dimethylbenz[alpha]anthracene-induced mammary tumor development in female rats.
Carcinogenesis
Identification of a noncanonical function for ribose-5-phosphate isomerase A promotes colorectal cancer formation by stabilizing and activating ?-catenin via a novel C-terminal domain.
Carcinoma, Basal Cell
Basal cell carcinoma with perineural invasion: reexcision perineural invasion?
Carcinoma, Hepatocellular
Ribose-5-Phosphate Isomerase A Overexpression Promotes Liver Cancer Development in Transgenic Zebrafish via Activation of ERK and ?-catenin Pathways.
Carcinoma, Hepatocellular
Ribose-5-phosphate isomerase A regulates hepatocarcinogenesis via PP2A and ERK signaling.
Carcinoma, Hepatocellular
[Experimental and clinical studies on ribosephosphate isomerase (author's transl)]
Cerebrovascular Disorders
MR regional perfusion imaging: visualizing functional collateral circulation.
Chagas Disease
Ribose 5-phosphate isomerase type B from Trypanosoma cruzi: kinetic properties and site-directed mutagenesis reveal information about the reaction mechanism.
Chagas Disease
Studying effects of different protonation states of His11 and His102 in ribose-5-phosphate isomerase of Trypanosoma cruzi: an example of cooperative behavior.
Colorectal Neoplasms
Arginine methylation of ribose-5-phosphate isomerase A senses glucose to promote human colorectal cancer cell survival.
Colorectal Neoplasms
Identification of a noncanonical function for ribose-5-phosphate isomerase A promotes colorectal cancer formation by stabilizing and activating ?-catenin via a novel C-terminal domain.
Cone-Rod Dystrophies
Retinitis pigmentosa inversa with unilateral high myopia with fellow eye optic disc pitting.
Cysts
Studies on the metabolism of Echinococcus granulosus. V. The phosphopentose isomerase of hydatid cyst scolices.
Diabetes Mellitus
Increased renal cortical stiffness obtained by share-wave elastography imaging significantly predicts the contrast-induced nephropathy in patients with preserved renal function.
Dyslipidemias
One Anastomosis Gastric Bypass/Minigastric Bypass in Patients with BMI < 35 kg/m2 and Type 2 Diabetes Mellitus: Preliminary Report.
Echinococcosis
Studies on the metabolism of Echinococcus granulosus. V. The phosphopentose isomerase of hydatid cyst scolices.
Endocarditis
In vivo activities and penetration of the two components of the streptogramin RP 59500 in cardiac vegetations of experimental endocarditis.
Hepatitis C
Dysregulated Erythropoietin, Hepcidin, and Bone Marrow Iron Metabolism Contribute to Interferon-Induced Anemia in Hepatitis C.
HIV Infections
Retrograde Peri-Implantitis: A Case Report Introducing An Approach to its Management.
Huntington Disease
Reduced neuronal expression of ribose-5-phosphate isomerase enhances tolerance to oxidative stress, extends lifespan, and attenuates polyglutamine toxicity in Drosophila.
Hypercholesterolemia
Rice protein isolate improves lipid and glucose homeostasis in rats fed high fat/high cholesterol diets.
Hypertension
Increased renal cortical stiffness obtained by share-wave elastography imaging significantly predicts the contrast-induced nephropathy in patients with preserved renal function.
Infections
Clinical significance of immature reticulocyte fraction determined by automated reticulocyte counting.
Infections
Comparative efficacies of procalcitonin and conventional inflammatory markers for prediction of renal parenchymal inflammation in pediatric first urinary tract infection.
Infections
Nonsurgical Endodontic Treatment of Necrotic Teeth Resolved Apical Lesions on Adjacent Implants with Retrograde/Apical Peri-implantitis: A Case Series with 2-year Follow-up.
Infections
Retrograde Peri-Implantitis: A Case Report Introducing An Approach to its Management.
Infections
Use of Postpartum Magnetic Resonance Imaging for Diagnosis and Classification of Retained Placenta Tissue.
Insulin Resistance
Rice protein isolate improves lipid and glucose homeostasis in rats fed high fat/high cholesterol diets.
Intellectual Disability
Formal Modeling of the Resistance to Peer Influence Questionnaire: A Comparison of Adolescent Boys and Girls With and Without Mild-to-Borderline Intellectual Disability.
Intermittent Claudication
Pathophysiologic classification of peripheral vascular disease by positional changes in regional transcutaneous oxygen tension.
Intermittent Claudication
Use of a transcutaneous PO2 regional perfusion index to quantify tissue perfusion in peripheral vascular disease.
Leishmaniasis, Visceral
Chemical- and thermal-induced unfolding of Leishmania donovani ribose-5-phosphate isomerase B: a single-tryptophan protein.
Leishmaniasis, Visceral
Mutational and Structural Analysis of Conserved Residues in Ribose-5-Phosphate Isomerase B from Leishmania donovani: Role in Substrate Recognition and Conformational Stability.
Leukoencephalopathies
Further Delineation of Ribose-5-phosphate Isomerase Deficiency: Report of a Third Case.
Leukoencephalopathies
Ribose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy.
Leukoencephalopathies
[A newly discovered metabolic diseases due to defects in the pentose pathway].
Liver Neoplasms
Ribose-5-Phosphate Isomerase A Overexpression Promotes Liver Cancer Development in Transgenic Zebrafish via Activation of ERK and ?-catenin Pathways.
Lupus Erythematosus, Systemic
Anti-RNA polymerase I antibodies in the sera of MRL lupus mice at the initial stages of disease are directed primarily against phosphorylation-dependent epitopes.
Meningioma
Assessment of Vascular Supply of Hypervascular Extra-Axial Brain Tumors with 3T MR Regional Perfusion Imaging.
Metabolic Syndrome
One Anastomosis Gastric Bypass/Minigastric Bypass in Patients with BMI < 35 kg/m2 and Type 2 Diabetes Mellitus: Preliminary Report.
Myelodysplastic Syndromes
Clinical significance of immature reticulocyte fraction determined by automated reticulocyte counting.
Myopia
Retinitis pigmentosa inversa with unilateral high myopia with fellow eye optic disc pitting.
Neoplasm Metastasis
[Experimental and clinical studies on ribosephosphate isomerase (author's transl)]
Neoplasms
A rice protein isolate alters 7,12-dimethylbenz[alpha]anthracene-induced mammary tumor development in female rats.
Neoplasms
Assessment of Vascular Supply of Hypervascular Extra-Axial Brain Tumors with 3T MR Regional Perfusion Imaging.
Neoplasms
Can multiparametric MRI and FDG-PET predict outcome in diffuse brainstem glioma? A report from a prospective phase-II study.
Neoplasms
Critical evaluation of the usefulness of different reticulocyte parameters in monitoring the erythropoiesis reaction to cancer chemotherapy.
Neoplasms
In vitro actions on human cancer cells and the liquid chromatography-mass spectrometry/mass spectrometry fingerprint of phytochemicals in rice protein isolate.
Neoplasms
The relative proliferation index as a more sensitive parameter for evaluating lymphoproliferative responses of cancer patients to mitogens and alloantigens.
Night Blindness
Retinitis pigmentosa inversa with unilateral high myopia with fellow eye optic disc pitting.
Osteoporosis
The inferomedial femoral neck is compromised by age but not disease: Fracture toughness and the multifactorial mechanisms comprising reference point microindentation.
Peri-Implantitis
Incidence of retrograde peri-implantitis in sites with previous apical surgeries: A retrospective study.
Peri-Implantitis
Nonsurgical Endodontic Treatment of Necrotic Teeth Resolved Apical Lesions on Adjacent Implants with Retrograde/Apical Peri-implantitis: A Case Series with 2-year Follow-up.
Periapical Periodontitis
Incidence of retrograde peri-implantitis in sites with previous apical surgeries: A retrospective study.
Peripheral Nervous System Diseases
Ribose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy.
Pre-Eclampsia
Erythrocyte changes in preeclampsia: relationship between maternal and cord blood erythrocyte damage.
Pressure Ulcer
Reproducibility of transcutaneous oxygen pressure measurements in persons with spinal cord injury.
Proteinuria
Erythrocyte changes in preeclampsia: relationship between maternal and cord blood erythrocyte damage.
ribose-5-phosphate isomerase deficiency
Analysis of polyols in urine by liquid chromatography-tandem mass spectrometry: A useful tool for recognition of inborn errors affecting polyol metabolism.
ribose-5-phosphate isomerase deficiency
Further Delineation of Ribose-5-phosphate Isomerase Deficiency: Report of a Third Case.
ribose-5-phosphate isomerase deficiency
Polyols accumulated in ribose-5-phosphate isomerase deficiency increase mitochondrial superoxide production and improve antioxidant defenses in rats' prefrontal cortex.
ribose-5-phosphate isomerase deficiency
Ribose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy.
ribose-5-phosphate isomerase deficiency
The difference between rare and exceptionally rare: molecular characterization of ribose 5-phosphate isomerase deficiency.
Tooth Loss
Retrograde peri-implantitis: evaluation and treatment protocols of a rare lesion.
transaldolase deficiency
Analysis of polyols in urine by liquid chromatography-tandem mass spectrometry: A useful tool for recognition of inborn errors affecting polyol metabolism.
Trypanosomiasis, African
Ribose 5-phosphate isomerase B knockdown compromises Trypanosoma brucei bloodstream form infectivity.
Tuberculosis
Backbone assignment of ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB).
Tuberculosis
Competitive inhibitors of Mycobacterium tuberculosis ribose-5-phosphate isomerase B reveal new information about the reaction mechanism.
Tuberculosis
Competitive inhibitors of type B ribose 5-phosphate isomerases: design, synthesis and kinetic evaluation of new D-allose and D-allulose 6-phosphate derivatives.
Tuberculosis
D-ribose-5-phosphate isomerase B from Escherichia coli is also a functional D-allose-6-phosphate isomerase, while the Mycobacterium tuberculosis enzyme is not.
Tuberculosis
Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site.
Urinary Tract Infections
Comparative efficacies of procalcitonin and conventional inflammatory markers for prediction of renal parenchymal inflammation in pediatric first urinary tract infection.
Virus Diseases
Clinical significance of immature reticulocyte fraction determined by automated reticulocyte counting.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
34
D-ribulose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
232
D-talose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
98
L-allose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
173
L-ribose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
319
L-ribulose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
125
L-tagatose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
106
D-allose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
53
D-psicose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
44
D-ribose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
0.017
D-ribose 5-phosphate
A0A4S5F2E5
pH 7.5, 65°C, recombinant enzyme
17
D-ribose 5-phosphate
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
0.015
D-ribulose 5-phosphate
A0A4S5F2E5
pH 7.5, 65°C, recombinant enzyme
5
D-ribulose 5-phosphate
in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30°C
15
D-ribulose 5-phosphate
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
37
L-talose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
additional information
additional information
dramatic increase of Km-value at temperatures above 80°C
-
additional information
additional information
-
dramatic increase of Km-value at temperatures above 80°C
-
additional information
additional information
-
kinetics with aldose and ketose substrates, recombinant enzyme, overview
-
additional information
additional information
A0A4S5F2E5
kinetics with aldose and ketose substrates, recombinant enzyme, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9193
D-ribulose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
119
D-talose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
1506
L-allose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
322
L-ribose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
17
L-ribulose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
1822
L-tagatose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
2682
D-allose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
2347
D-psicose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
11880
D-ribose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
52000
D-ribose 5-phosphate
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
52000
D-ribose 5-phosphate
A0A4S5F2E5
pH 7.5, 65°C, recombinant enzyme
2 - 8
D-ribulose 5-phosphate
in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30°C
39530
D-ribulose 5-phosphate
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
39530
D-ribulose 5-phosphate
A0A4S5F2E5
pH 7.5, 65°C, recombinant enzyme
13420
L-talose
A0A4S5F2E5
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2589
D-ribulose 5-phosphate
A0A4S5F2E5
pH 7.5, 65°C, recombinant enzyme
3029
D-ribose 5-phosphate
A0A4S5F2E5
pH 7.5, 65°C, recombinant enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.009
5-phospho-D-ribonate
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
15
D-Allose 6-phosphate
in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30°C
0.34
N-(5-phospho-D-ribonoyl)-glycine
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
1.9
N-(5-phospho-D-ribonoyl)-hydrazine
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
0.04
5-phospho-D-ribonamide
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.07
5-phospho-D-ribonamide
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.09
5-phospho-D-ribonohydroxamic acid
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.26
5-phospho-D-ribonohydroxamic acid
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.43
5-phospho-D-ribonohydroxamic acid
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
0.11
N-(5-phospho-D-ribonoyl)-methylamine
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.18
N-(5-phospho-D-ribonoyl)-methylamine
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.3
D-allulose 6-phosphate
Mycobacterium tuberculosis
in 50 mM Tris-HCl, pH 7.5, at 37°C
1
N-(5-phospho-D-ribonoyl)-hydrazine
Mycobacterium tuberculosis
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.2
5-phospho-D-ribonamide
Escherichia coli
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.22
5-phospho-D-ribonamide
Mycobacterium tuberculosis
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
1.33
5-phospho-D-ribonamide
Escherichia coli
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
0.031
5-phospho-D-ribonate
Mycobacterium tuberculosis
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
1.31
5-phospho-D-ribonate
Escherichia coli
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.17
5-phospho-D-ribonohydroxamic acid
Escherichia coli
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.44
5-phospho-D-ribonohydroxamic acid
Mycobacterium tuberculosis
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.62
5-phospho-D-ribonohydroxamic acid
Escherichia coli
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
1.42
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
Mycobacterium tuberculosis
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
1.6
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
Escherichia coli
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
2
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
Escherichia coli
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.57
N-(5-phospho-D-ribonoyl)-glycine
Mycobacterium tuberculosis
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
9
N-(5-phospho-D-ribonoyl)-glycine
Escherichia coli
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.19
N-(5-phospho-D-ribonoyl)-methylamine
Mycobacterium tuberculosis
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.35
N-(5-phospho-D-ribonoyl)-methylamine
Escherichia coli
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
0.36
N-(5-phospho-D-ribonoyl)-methylamine
Escherichia coli
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
additional information
additional information
Trypanosoma cruzi
IC50 values of 5-phospho-D-ribonohydroxamic acid and 4-phospho-D-erythronhydrazide are above 10 mM
-
additional information
additional information
Trypanosoma cruzi
-
IC50 values of 5-phospho-D-ribonohydroxamic acid and 4-phospho-D-erythronhydrazide are above 10 mM
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.058
-
using D-glucose 6-phosphate as substrate, at 35°C and pH 7.5
0.21
A0A4S5F2E5
purified enzyme, using D-tagatose as substrate, at 65°C and pH 7.5
0.259
mutant enzyme H98A, using D-psicose as substrate, pH 7.5, 80°C
0.299
0.53
A0A4S5F2E5
purified enzyme, using L-allose as substrate, at 65°C and pH 7.5
0.698
mutant enzyme N99A, using D-psicose as substrate, pH 7.5, 80°C
0.917
mutant enzyme T67A, using D-psicose as substrate, pH 7.5, 80°C
1.256
mutant enzyme H9A, using D-psicose as substrate, pH 7.5, 80°C
1.815
mutant enzyme T135A, using D-psicose as substrate, pH 7.5, 80°C
1.994
wild type enzyme, using D-psicose as substrate, pH 7.5, 80°C
1037
12
A0A4S5F2E5
purified enzyme, using L-psicose as substrate, at 65°C and pH 7.5
1352
19680
2.313
mutant enzyme R132A, using D-psicose as substrate, pH 7.5, 80°C
25690
272
A0A4S5F2E5
purified enzyme, using L-ribose as substrate, at 65°C and pH 7.5
50
A0A4S5F2E5
purified enzyme, using D-talose as substrate, at 65°C and pH 7.5
5374
5800
600
A0A4S5F2E5
purified enzyme, using L-allose as substrate, at 65°C and pH 7.5
720
A0A4S5F2E5
purified enzyme, using L-ribulose as substrate, at 65°C and pH 7.5
7363
additional information
0.299
mutant enzyme H133A, using D-psicose as substrate, pH 7.5, 80°C
0.299
mutant enzyme R136A, using D-psicose as substrate, pH 7.5, 80°C
1037
A0A4S5F2E5
purified enzyme, using D-psicose as substrate, at 65°C and pH 7.5
1037
A0A4S5F2E5
purified recombinant enzyme, substrate D-psicose
1352
A0A4S5F2E5
purified enzyme, using D-allose as substrate, at 65°C and pH 7.5
1352
A0A4S5F2E5
purified recombinant enzyme, substrate D-allose
19680
A0A4S5F2E5
purified enzyme, using D-ribulose 5-phosphate as substrate, at 65°C and pH 7.5
19680
A0A4S5F2E5
purified recombinant enzyme, substrate D-ribulose 5-phosphate
25690
A0A4S5F2E5
purified enzyme, using D-ribose 5-phosphate as substrate, at 65°C and pH 7.5
25690
A0A4S5F2E5
purified recombinant enzyme, substrate D-ribose 5-phosphate
5374
A0A4S5F2E5
purified enzyme, using D-ribulose as substrate, at 65°C and pH 7.5
5374
A0A4S5F2E5
purified recombinant enzyme, substrate D-ribulose
5800
A0A4S5F2E5
purified enzyme, using D-ribose as substrate, at 65°C and pH 7.5
5800
A0A4S5F2E5
purified recombinant enzyme, substrate D-ribose
7363
A0A4S5F2E5
purified enzyme, using L-talose as substrate, at 65°C and pH 7.5
7363
A0A4S5F2E5
purified recombinant enzyme, substrate L-talose
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
6 - 9.9
-
pH 6: about 40% of maximal activity, pH 9.9: about 65% of maximal activity
6 - 9
-
more than 80% of its maximal activity is maintained at pH values from 6.0 to 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
65
70
80
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 99
-
enzyme activity increases significantly when the temperature increases until 80°C. The optimum temperature is 80°C. The activity at 30°C is 25% of that at 80°C. The enzyme activity decreases after 80°C. It is still highly active when the temperature reaches 99°C, 90% activity of that of 80°C. This enzyme shows relatively high activity (above 50% of its maximum activity) over a large temperature range of 40-99°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
physical interaction between phosphoribulokinase and phosphoriboisomerase in the presence of substrate
-
-
brenda
two enzyme forms: constitutive isomerase A and inducible isomerase B
-
-
brenda
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
-
-
brenda
phosphoribulokinase and phosphoriboisomerase are associated to a complex
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
in colon cancer cell lines, RPIA enters the nucleus to form a complex with the adenomatous polyposis coli and beta-catenin
brenda
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co-localization of enzyme with phosphoribulokinase and Rubisco
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
deficiency in a cytosolic ribose-5-phosphate isomerase causes chloroplast dysfunction, late flowering and premature cell death in Arabidopsis thaliana
metabolism
physiological function
metabolism
-
ribose 5-phosphate isomerase is a key enzyme of the pentose phosphate pathway
metabolism
ribose 5-phosphate isomerase is a key enzyme of the pentose phosphate pathway
metabolism
A0A4S5F2E5
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
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
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
metabolism
-
ribose 5-phosphate isomerase is a key enzyme of the pentose phosphate pathway
physiological function
gene is essential for parasite survival. Mutant promastigotes complemented with an episomal copy of RpiB carrying a mutation that abolishes isomerase activity exhibit no defect in growth, metacyclogenesis or macrophage infection. An impairment in intracellular amastigotes' replication is observed in these mutants, and mice infected withthe mutants have a reduced parasite burden in the liver
physiological function
knockdown or genomic deletion of RPIA results in an increase of ATG4B proteases-mediated processing of autosome marker protein LC3 and in the appearance of LC3-positive autophagosomes in cells. Increased LC3 processing upon knockdown of RPIA can be reversed by treatment with N-acetyl cysteine
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)