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Information on EC 5.3.1.5 - xylose isomerase and Organism(s) Streptomyces rubiginosus and UniProt Accession P24300
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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: Streptomyces rubiginosus
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
-
-
-
-
D-xylose isomerase
D-Xylose ketoisomerase
-
-
-
-
D-xylulose keto-isomerase
-
-
-
-
Isomerase, xylose
-
-
-
-
Optisweet
Swetase
-
-
-
-
XI
D-xylose isomerase
-
-
-
-
XI
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
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
-
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
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
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glyceraldehyde
competitive inhibition of the isomerization of D-xylose
D-Threonohydroxamic acid
competitive inhibitor, complete inhibition at 0.5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
D-glyceraldehyde
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
4.9
D-xylose
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
180
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D81A and wild-type
200
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q
310
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutants E221A and D56N
1 - 4
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
1 - 1.2
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
3
D-xylose
-
native wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
3.4
D-xylose
-
mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
3.8
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
4 - 5
D-xylose
-
mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
4.3
D-xylose
-
mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
5
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
5.3
D-xylose
-
mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
6
D-xylose
-
mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
6.5
D-xylose
-
mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
7.4
D-xylose
-
mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
8
D-xylose
-
mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
10
D-xylose
-
mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
15
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
27
D-xylose
-
mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
33
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
37
D-xylose
-
mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
42
D-xylose
-
mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
83
D-xylose
-
native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
548
D-xylose
-
mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
D-glyceraldehyde
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
2.4
D-xylose
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
0.03 - 0.55
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant E221A
0.031 - 0.51
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D56N
3 - 6
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q
3.02
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q
0.007
D-xylose
-
mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.056
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.064
D-xylose
-
mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.07
D-xylose
-
mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.074
D-xylose
-
mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.11
D-xylose
-
mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.14
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.15
D-xylose
-
mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.18
D-xylose
-
mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.19
D-xylose
-
mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.31
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.33
D-xylose
-
mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.41
D-xylose
-
native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.51
D-xylose
-
mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.66
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.8
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.96
D-xylose
-
mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
1.22
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
1.38
D-xylose
-
mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
2.3
D-xylose
-
mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
5.52
D-xylose
-
native wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000034
D-glyceraldehyde
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
0.49
D-xylose
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
0.00013
D-xylose
-
mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0018
D-xylose
-
mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0019
D-xylose
-
mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0024
D-xylose
-
mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0037
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0049
D-xylose
-
native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.007
D-xylose
-
mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0094
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.01
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.018
D-xylose
-
mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.019
D-xylose
-
mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.023
D-xylose
-
mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.024
D-xylose
-
mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.059
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.064
D-xylose
-
mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.181
D-xylose
-
mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.211
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.24
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.321
D-xylose
-
mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.676
D-xylose
-
mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
1.84
D-xylose
-
native wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 8.2
-
in presence of Mg2+ and Co2+, mutants D65A and D163N/E167Q
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of the location of hydrogen atoms by time-of-flight neutron Laue technique. The neutron structure of crystalline XI with bound product, D-xylulose, shows, that O5 of D-xylulose is not protonated but is hydrogen-bonded to doubly protonated His54. Also, Lys289, which is neutral in native XI, is protonated, while the catalytic water in native XI has become activated to a hydroxyl anion which is in the proximity of C1 and C2, the molecular site of isomerization of xylose
in complex with D-glyceraldehyde, hanging drop vapor diffusion method, using 0.2-0.3 M Mg-formate at pH 7.0 and 22°C
structure of E186Q mutant with cyclic glucose bound at the active site, to 2.2 A resolution. Residue His54 is doubly protonated and is poised to protonate the glucose O5 position, while Lys289, which is neutral, promotes deprotonation of the glucose O1H hydroxyl group via an activated water molecule. An extended hydrogen-bonding network connects the conserved residues Lys289 and Lys183 through three structurally conserved water molecules and residue 186
study on the dynamics of solute transport in orthorhombic D-xylose isomerase crystals by means of Brownian dynamics and molecular dynamics simulations and investigation of the diffusion of S-phenylglycine molecules inside XI crystals. The S-phenylglycine molecules mostly interact with residues His54, Asp287, and Lys183. In general, the diffusivities of solute species are found to be 1 to 2 orders of magnitude lower than those of the corresponding free molecules in water
the mechanism of ring-opening for L-arabinose is the same as for the reaction with D-xylose. In the reactive Michaelis complex L-arabinose is distorted to the high-energy 5S1 conformation. Amino acid substitutions in a hydrophobic pocket near C5 of L-arabinose can enhance sugar binding. L-ribulose and L-ribose are found in furanose forms when bound to the enzyme
time-of-flight neutron diffraction at 1.8 A resolution, metal-free enzyme - emphasis on the active site of xylose isomerase, especially of protonation states of His, Lys and H2O
neutron diffraction, largest crystals at 18°C, 95 mg/ml xylose isomerase, 16.9% ammonium sulfate, mathematical analysis to determine optimal conditions for crystallization
-
neutron quasi-Laue diffraction, resolution: 2.2 A - clear visibility of deuterium atoms, clarification of critical residues at the active site and their protonation states
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D163N/E167Q
-
40-60% of wild-type activity, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
D56N
-
turnover number increased by 30-40% over that ofwild-type at pH 7.3, lower pH optimum than wild-type, nearly same thermostability as wild-type
D65A
-
40-60% of wild-type activity, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
D81A
-
40-60% of wild-type activity, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
E221A
-
turnover number increased by 30-40% over that from wild-type at pH 7.3, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
H220S
-
decreased affinity for Mg2+ and decraesed activity in contrast to wild-type
N185K
-
decreased affinity for Mg2+ and decraesed activity in contrast to wild-type
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
-
70-80% of cross-linked crystalline xylose isomerase activity is left after incubation for 24 h at 50°C in buffer solutions (pH 7.2) containing 10-90% acetone. Soluble xylose isomerase is considerably less stable in acetone-containing solutions. The addition of acetone enhances the production of fructose from glucose by enhancing the reaction rate and shifting the equilibrium toward fructose. However, xylose isomerase must be in the form of cross-linked crystals for maximal activity and stability
Ethanol
-
in buffer containing 50% ethanol only 2% of the initial cross-linked crystalline xylose isomerase activity is retained after 24 h at 50°C. Soluble xylose isomerase is considerably less stable in ethanol-containing solutions
Methanol
-
cross-linked crystalline xylose isomerase is inactivated in 24 h at 50°C even more in maleate buffer containing 50% methanol
Pyridine
-
cross-linked crystalline xylose isomerase is inactivated in 24 h at 50°C even more in maleate buffer containing 10% pyridine
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from a stock solution of a food grade product, 2 counterdiffusion dialysis devices: diffusion-controlled apparatus for microgravity and counterdiffusion cell, growth of crystals approx. 3 months
gel filtration over Sephacryl S200 - dialysis against 0.05 g/l MgSO4, purity control verified with capillary electrophoresis
-
gel filtration with Sephacryl S-200 high resolution media, running buffer composed of 0.05 M sodium phosphate pH 7.7, 0.1 M sodium chloride and 0.02% azide - final purity of xylose isomerase: 96%
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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
Carrell, H.L.; Rubin, B.H.; Hurley, T.J.; Glusker, J.P.
X-ray crystal structure of D-xylose isomerase at 4-A resolution
J. Biol. Chem.
259
3230-3236
1984
Streptomyces rubiginosus
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
Vuolanto, A.; Uotila, S.; Leisola, M.; Visuri, K.
Solubility and crystallization of xylose isomerase from Streptomyces rubiginosus
J. Crystal Growth
257
403-411
2003
Streptomyces rubiginosus
-
Cha, J.
Contribution of second metal binding site for metal specificity of D-xylose isomerase
J. Microbiol. Biotechnol.
9
757-763
1999
Streptomyces rubiginosus
-
Cha, J.; Batt, C.A.
Lowering the pH optimum of D-xylose isomerase: the effect of mutations of the negatively charged residues
Mol. Cells
8
374-382
1998
Streptomyces rubiginosus
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
-
Hanson, B.L.; Langan, P.; Katz, A.K.; Li, X.; Harp, J.M.; Glusker, J.P.; Schoenborn, B.P.; Bunick, G.J.
A preliminary time-of-flight neutron diffraction study of Streptomyces rubiginosus D-xylose isomerase
Acta Crystallogr. Sect. D
60
241-249
2004
Streptomyces rubiginosus
Vilonen, K.M.; Vuolanto, A.; Jokela, J.; Leisola, M.S.; Krause, A.O.
Enhanced glucose to fructose conversion in acetone with xylose isomerase stabilized by crystallization and cross-linking
Biotechnol. Prog.
20
1555-1560
2004
Streptomyces rubiginosus
Karimaki, J.; Parkkinen, T.; Santa, H.; Pastinen, O.; Leisola, M.; Rouvinen, J.; Turunen, O.
Engineering the substrate specificity of xylose isomerase
Protein Eng. Des. Sel.
17
861-869
2004
Actinoplanes missouriensis, Streptomyces rubiginosus (P24300), Streptomyces rubiginosus
Meilleur, F.; Snell, E.H.; van der Woerd, M.J.; Judge, R.A.; Myles, D.A.
A quasi-Laue neutron crystallographic study of D-xylose isomerase
Eur. Biophys. J.
35
601-609
2006
Streptomyces rubiginosus
Snell, E.H.; van der Woerd, M.J.; Damon, M.; Judge, R.A.; Myles, D.A.; Meilleur, F.
Optimizing crystal volume for neutron diffraction: D-xylose isomerase
Eur. Biophys. J.
35
621-632
2006
Streptomyces rubiginosus
Katz, A.K.; Li, X.; Carrell, H.L.; Hanson, B.L.; Langan, P.; Coates, L.; Schoenborn, B.P.; Glusker, J.P.; Bunick, G.J.
Locating active-site hydrogen atoms in D-xylose isomerase: time-of-flight neutron diffraction
Proc. Natl. Acad. Sci. USA
103
8342-8347
2006
Streptomyces rubiginosus (P24300), Streptomyces rubiginosus
Kovalevsky, A.Y.; Katz, A.K.; Carrell, H.L.; Hanson, L.; Mustyakimov, M.; Fisher, S.Z.; Coates, L.; Schoenborn, B.P.; Bunick, G.J.; Glusker, J.P.; Langan, P.
Hydrogen location in stages of an enzyme-catalyzed reaction: time-of-flight neutron structure of D-xylose isomerase with bound D-xylulose
Biochemistry
47
7595-7597
2008
Streptomyces rubiginosus (P24300)
Malek, K.; Coppens, M.O.
Molecular simulations of solute transport in xylose isomerase crystals
J. Phys. Chem. B
112
1549-1554
2008
Streptomyces rubiginosus (P24300)
Kovalevsky, A.Y.; Hanson, L.; Fisher, S.Z.; Mustyakimov, M.; Mason, S.A.; Forsyth, V.T.; Blakeley, M.P.; Keen, D.A.; Wagner, T.; Carrell, H.L.; Katz, A.K.; Glusker, J.P.; Langan, P.
Metal ion roles and the movement of hydrogen during reaction catalyzed by D-xylose isomerase: a joint x-ray and neutron diffraction study
Structure
18
688-699
2010
Streptomyces rubiginosus (P24300)
Toteva, M.M.; Silvaggi, N.R.; Allen, K.N.; Richard, J.P.
Binding energy and catalysis by D-xylose isomerase: kinetic, product, and X-ray crystallographic analysis of enzyme-catalyzed isomerization of (R)-glyceraldehyde
Biochemistry
50
10170-10181
2011
Streptomyces rubiginosus (P24300)
Waltman, M.; Yang, Z.; Langan, P.; Graham, D.; Kovalevsky, A.
Engineering acidic Streptomyces rubiginosus D-xylose isomerase by rational enzyme design
Protein Eng.
27
59-64
2014
Streptomyces rubiginosus
Munshi, P.; Snell, E.H.; van der Woerd, M.J.; Judge, R.A.; Myles, D.A.; Ren, Z.; Meilleur, F.
Neutron structure of the cyclic glucose-bound xylose isomerase E186Q mutant
Acta Crystallogr. Sect. D
70
414-420
2014
Streptomyces rubiginosus (P24300)
Langan, P.; Sangha, A.K.; Wymore, T.; Parks, J.M.; Yang, Z.K.; Hanson, B.L.; Fisher, Z.; Mason, S.A.; Blakeley, M.P.; Forsyth, V.T.; Glusker, J.P.; Carrell, H.L.; Smith, J.C.; Keen, D.A.; Graham, D.E.; Kovalevsky, A.
L-Arabinose binding, isomerization, and epimerization by D-xylose isomerase X-ray/neutron crystallographic and molecular simulation study
Structure
22
1287-1300
2014
Streptomyces rubiginosus (P24300)
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