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Information on EC 5.3.1.5 - xylose isomerase and Organism(s) Actinoplanes missouriensis and UniProt Accession P12851
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5.3.1.5 xylose isomeraseIUBMB Comments
Contains two divalent metal ions, preferably magnesium, located at different metal-binding sites within the active site. The enzyme catalyses the interconversion of aldose and ketose sugars with broad substrate specificity. The enzyme binds the closed form of its sugar substrate (in the case of xylose and glucose, only the alpha anomer ) and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism.
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Word Map
- 5.3.1.5
-
isomerization
- biomass
- d-glucose
- xylitol
- xylulokinase
- pentose
-
lignocellulosic
- isomerases
- syrup
- corn
- gi
- d-fructose
- rubiginosus
-
bioethanol
- piromyces
- arthrobacter
- l-arabinose
- synthesis
- actinoplanes
-
high-fructose
-
xylose-fermenting
- transaldolase
-
saccharification
- thermoanaerobacter
-
co-fermentation
-
hemicellulosic
- thermoanaerobacterium
- neapolitana
- stipitis
- energy production
- orpinomyces
- thermosulfurogenes
-
xylose-utilizing
-
diauxic
- food industry
- nutrition
- biotechnology
- degradation
The taxonomic range for the selected organisms is: Actinoplanes missouriensis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
xylose isomerase, glucose isomerase, d-xylose isomerase, spezyme, xylose (glucose) isomerase, glucose/xylose isomerase, sdxyi, tthxi, tcaxi, sweetzyme, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-xylose aldose-ketose-isomerase
-
-
-
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D-xylose isomerase
-
-
-
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D-Xylose ketoisomerase
-
-
-
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D-xylulose keto-isomerase
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-
-
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Isomerase, xylose
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-
-
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Maxazyme
Swetase
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-
-
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XI
XI
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-xylopyranose aldose-ketose-isomerase
Contains two divalent metal ions, preferably magnesium, located at different metal-binding sites within the active site. The enzyme catalyses the interconversion of aldose and ketose sugars with broad substrate specificity. The enzyme binds the closed form of its sugar substrate (in the case of xylose and glucose, only the alpha anomer [4]) and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism.
CAS REGISTRY NUMBER
COMMENTARY
9023-82-9
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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
L-ribose
?
-
no increased reaction rate observed for mutant F26W
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
additional information
-
two metal sites: metal site 1 is four-coordinated and tetrahedral in the absence of substrate and is six-coordinated and octahedral in its presence, the O2 and O4 atoms of the linear inhibitors and substrate bind to the metal 1. Metal site 2 is octahedral in all cases, its position changes by 0.7 A when it binds O1 of the substrate and by more than 1 A when it also binds O2
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km-values for wild-type enzyme and mutants E186D and E186Q, activated by Mg2+, Mn2+ or Co2+
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
turnover numbers for wild-type enzyme and mutant enzymes E186D and E186Q, activated by Mg2+, Mn2+ or Co2+
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.25
-
mutant E186Q, xylose isomerization, activated by Mn2+ or Mg2+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of a number of binary and ternary complexes involving wild-type and mutant enzymes, the divalent cations Mg2+, Co2+, or Mn2+ and either the substrate xylose or substrate analogs
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V135N
no effect on the reaction with D-xylose and L-arabinose, reaction efficiency with L-ribose is increased 2-4fold, reaction with D-glucose is impaired
E186D
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mutant enzymes E186D and E186Q are active, and their metal specificity is different from that of the wild type. The E186 enzyme is most active with Mn2+ and has a drastically shifted pH optimum
E186Q
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mutant enzymes E186D and E186Q are active, and their metal specificity is different from that of the wild type. The E186 enzyme is most active with Mn2+ and has a drastically shifted pH optimum
E253K
-
substitution of Arg for Lys at position 253 at the dimer-dimer interface increases the half-life of the enzyme by 30%. The largest stability gain is achieved in a triple mutant G70S/A73S/G74T
H101F
-
substitution of His101 by Phe abolishes the enzyme activity, whereas substitution of other His residues has no effect
H41L
-
substitution of Lys for His41 results in a mutant with near wild-type properties. This mutation completely abolishes adsorption to iminodiacetic acid-Cu(II)
Q256D
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catalytic efficiency with L-arabinose is increased 3fold, reaction rate with L-ribose is increased 6fold
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
-
mutant Q256D remains fully active for 60 min at 65°C, whereas the activity is rapidly lost at 80°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, by heat precipitation and cation exchange, proteins were 95% pure when estimated in SDS-PAGE
one-step purification by high-performance immobilized copper-affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
used in industry for the production of high-fructose corn syrups
synthesis
-
commercial importance in the production of high-fructose corn syrup, potential application in the production of ethanol from hemicelluloses
synthesis
-
production of fructose, which is used as an alternate sugar to sucrose or invert sugar in the food and beverage industries, it is also used in the baking and dairy industry
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mrabet, N.T.
One-step purification of Actinoplanes missouriensis D-xylose isomerase by high-performance immobilized copper-affinity chromatography: functional analysis of surface histidine residues by site-directed mutagenesis
Biochemistry
31
2690-2702
1992
Actinoplanes missouriensis
Jenkins, J.; Janin, J.; Rey, F.; Chiadmi, M.; van Tilbeurgh, H.; Lasters, I.; de Maeyer, M.; van Belle, D.; Wodak, S.J.; Lauwereys, M.; Stanssens, P.; Mrabet, N.T.; Snauwaert, J.; Matthyssens, G.; Lambeir, A.M.
Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites
Biochemistry
31
5449-5458
1992
Actinoplanes missouriensis
Van Tillbeurgh, H.; Jenkins, J.; Chiadmi, M.; Janin, J.; Wodak, S.J.; Mrabet, N.T.; Lambeir, A.M.
Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 3. Changing metal specificity and the pH profile by site-directed mutagenesis
Biochemistry
31
5467-5471
1992
Actinoplanes missouriensis
Bhosale, S.H.; Rao, M.B.; Deshpande, V.V.
Molecular industrial aspects of glucose isomerase
Microbiol. Rev.
60
280-300
1996
Actinomyces olivocinereus, Actinoplanes missouriensis, Actinoplanes sp., Aerobacter levanicum, Aeromonas hydrophila, Arthrobacter sp., Bacillus licheniformis, Brevibacterium helvolum, Brevibacterium pentosoaminoacidicum, Citrobacter freundii, Citrobacter intermedius, Corynebacterium sp., Desemzia incerta, Enterobacter cloacae, Escherichia coli, Gordonia rubripertincta, Klebsiella aerogenes, Lactiplantibacillus pentosus, Lactiplantibacillus plantarum, Lactobacillus gayonii, Lactobacillus lycopersici, Lactobacillus mannitopoeus, Lentilactobacillus buchneri, Leuconostoc mesenteroides, Limosilactobacillus fermentum, Microbacterium arborescens, Microbispora rosea, Micromonospora coerulea, Mycobacterium sp., Nocardia asteroides, Nocardiopsis dassonvillei, Paracolobacterium aerogenoides, Priestia megaterium, Pseudonocardia sp., Sarcina sp., Sphingomonas paucimobilis, Streptococcus venuceus, Streptomyces achromogenes, Streptomyces bikiniensis, Streptomyces bobili, Streptomyces californicus, Streptomyces echinatus, Streptomyces flaveus, Streptomyces flavovirens, Streptomyces fradiae, Streptomyces glaucescens, Streptomyces griseofuscus, Streptomyces griseolus, Streptomyces griseus, Streptomyces matensis, Streptomyces nivens, Streptomyces olivaceus, Streptomyces olivochromogenes, Streptomyces phaeochromogenes, Streptomyces platensis, Streptomyces roseochromogenus, Streptomyces rubiginosus, Streptomyces venezuelae, Streptomyces virginiae, Streptomyces wedmorensis, Streptosporangium album, Streptosporangium vulgare, Thermoanaerobacter thermohydrosulfuricus, Thermoanaerobacterium thermosulfurigenes, Thermopolyspora sp., Thermus thermophilus, Weizmannia coagulans, Xanthomonas sp., Zymomonas mobilis
Straatsma, J.; Vellenga, K.; Witt, H.G.J.de; Joosten, G.E.
Isomerization of glucose to fructose. 2. Optimization of reaction conditions in the production of high fructose syrup by isomerization of glucose catalyzed by a whole cell immobilized glucose isomerase catalyst
Ind. Eng. Chem. Process Des. Dev.
22
356-361
1983
Streptomyces phaeochromogenes, Actinoplanes missouriensis, Weizmannia coagulans, Streptomyces rubiginosus
-
Santa, H.; Kammonen, J.; Lehtonen, O.; Karimaki, J.; Pastinen, O.; Leisola, M.; Turunen, O.
Stochastic boundary molecular dynamics simulation of L-ribose in the active site of Actinoplanes missouriensis xylose isomerase and its Val135Asn mutant with improved reaction rate
Biochim. Biophys. Acta
1749
65-73
2005
Actinoplanes missouriensis (P12851), Actinoplanes missouriensis
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