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Information on EC 5.3.1.5 - xylose isomerase and Organism(s) Streptomyces olivochromogenes and UniProt Accession P15587

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IUBMB 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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Streptomyces olivochromogenes
UNIPROT: P15587
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The taxonomic range for the selected organisms is: Streptomyces olivochromogenes
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
xylose isomerase, glucose isomerase, d-xylose isomerase, spezyme, xylose (glucose) isomerase, glucose/xylose isomerase, sdxyi, tthxi, tcaxi, sweetzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-xylose aldose-ketose-isomerase
-
-
-
-
D-xylose isomerase
-
-
-
-
D-Xylose ketoisomerase
-
-
-
-
D-xylulose keto-isomerase
-
-
-
-
Isomerase, xylose
-
-
-
-
Swetase
-
-
-
-
XI
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 hide
9023-82-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
r
D-Fructose
?
show the reaction diagram
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
essential for activity, there are two manganese atoms visible in the atomic resolution study
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
inactivates the enzyme
D-Threonohydroxamic acid
-
slow-binding competitive inhibitor with glucose as substrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
200 - 220
D-fructose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
pH 6: about 35% of maximal activity, pH 10: about 30% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
XYLA_STROL
387
0
42923
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
115000 - 117000
-
low speed sedimentation without reaching equilibrium, equilibrium sedimentation
56000
-
2 * 56000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 56000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3.0 A crystal structure
-
D-threonohydroxamic acid soaked into the crystal, crystallographic structure at 1.6 A resolution
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X-ray crystallographic structure of the metal-activated enzyme with the substrates D-glucose, 3-O-methyl-D-glucose and in the absence of substrate at 1.96 A, 2.19 A, and 1.81 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Z180L
-
one of the metal-binding sites, M-1, is removed by substitution of Glu-180 by Lys. Glu-180 is essential for isomerization but not for ring opening
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
room temperature, 30 min, stable above
2739
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
30 min, stable
65
-
30 min, about 50% loss of activity
70
-
30 min, about 70% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli HB101
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
commercial importance in the production of high-fructose corn syrup, potential application in the production of ethanol from hemicelluloses
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Suekane, M.; Tamura, M.; Tomimura, Ch.
Physico-chemical and enzymatic properties of purified glucose isomerases from Streptomyces olivochromogenes and Bacillus stearothermophilus
Agric. Biol. Chem.
42
909-917
1978
Geobacillus stearothermophilus, Streptomyces olivochromogenes
-
Manually annotated by BRENDA team
Farber, G.K.; Petsko, G.A.; Ringe, D.
The 3.0 A crystal structure of xylose isomerase from Streptomyces olivochromogenes
Protein Eng.
1
459-466
1987
Streptomyces olivochromogenes
Manually annotated by BRENDA team
Allen, K.N.; Lavie, A.; Petsko, G.A.; Ringe, D.
Design, synthesis, and characterization of a potent xylose isomerase inhibitor, D-threonohydroxamic acid, and high-resolution X-ray crystallographic structure of the enzyme-inhibitor complex
Biochemistry
34
3742-3749
1995
Streptomyces olivochromogenes
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Lavie, A.; Allen, K.N.; Petsko, G.A.; Ringe, D.
X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis
Biochemistry
33
5469-5480
1994
Streptomyces olivochromogenes
Manually annotated by BRENDA team
Fenn, T.D.; Ringe, D.; Petsko, G.A.
Xylose isomerase in substrate and inhibitor michaelis states: atomic resolution studies of a metal-mediated hydride shift
Biochemistry
43
6464-6474
2004
Streptomyces olivochromogenes (P15587), Streptomyces olivochromogenes
Manually annotated by BRENDA team