Information on EC 5.3.1.5 - Xylose isomerase

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

EC NUMBER
COMMENTARY
5.3.1.5
-
RECOMMENDED NAME
GeneOntology No.
Xylose isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-xylopyranose = D-xylulose
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
isomerization
-
-
isomerization
P15587
-
isomerization
-
-
isomerization
-
-
isomerization
-
-
isomerization
-
-
isomerization
-
-
isomerization
Arthrobacter nicotianae BIM B-5, Arthrobacter nicotianae BIM V-5, Bacteroides stercoris HJ-15, Escherichia coli DH5alpha, Escherichia coli HB101xylA, Lactococcus lactis 210 (Xyl-), Lactococcus lactis IO-1 (Xyl+), Pectobacterium atrosepticum jn42xylA
-
-
-
isomerization
Streptomyces corchorusii J-59
-
;
-
PATHWAY
KEGG Link
MetaCyc Link
Fructose and mannose metabolism
-
Metabolic pathways
-
Pentose and glucuronate interconversions
-
xylose degradation I
-
SYSTEMATIC NAME
IUBMB Comments
D-xylose 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 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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D-Xylose isomerase
-
-
-
-
D-Xylose isomerase
-
-
D-Xylose isomerase
P24300
-
D-Xylose ketoisomerase
-
-
-
-
D-Xylose ketoisomerase
-
-
D-Xylose ketoisomerase
Arthrobacter nicotianae BIM V-5
-
-
-
D-xylose ketol isomerase
-
-
D-xylose ketol-isomerase
Opuntia ficus-indica, Opuntia vulgaris
-
-
D-xylose ketol-isomerase
-
-
D-xylose ketol-isomerase
Streptomyces corchorusii J-59
-
-
-
D-xylose ketol-isomerase
-
-
D-xylose: ketol-isomerase
-
-
D-xylose: ketol-isomerase
Arthrobacter nicotianae BIM B-5
-
-
-
D-xylose: ketol-isomerase
-
-
D-xylose: ketol-isomerase
Escherichia coli HB101xylA
-
-
-
D-xylose: ketol-isomerase
-
-
D-xylose: ketol-isomerase
Pectobacterium atrosepticum jn42xylA
-
-
-
D-xylulose keto-isomerase
-
-
-
-
glucose isomerase
-
-
glucose/xylose isomerase
-
-
glucose/xylose isomerase
Streptomyces sp. NCIM 2730
-
-
-
GXI
Streptomyces sp. NCIM 2730
-
-
-
Isomerase, xylose
-
-
-
-
Maxazyme
-
Gist Brocades and Anheuser-Busch Inc.
Optisweet
-
Miles Kali-Chemie
SDXyI
Streptomyces diastaticus No. 7
-
-
SDXyI
Streptomyces diastaticus No. 7 M1033
-
-
-
Spezyme
-
Finnsugar
Sweetzyme
-
-
Sweetzyme
-
Novo-Nordisk
Sweetzyme Q
-
-
Swetase
-
-
-
-
T80 xylose isomerase
-
a thermostable isozyme
XI
-
-
-
-
XI
Lactococcus lactis 210 (Xyl-), Lactococcus lactis IO-1 (Xyl+)
-
-
-
XYLA
Thermoanaerobacter ethanolicus JW200 (ATCC 31550)
D2DK62
-
-
XYLA
Thermotoga neapolitana 5068
-
-
-
XYLA
C7G532
-
XYLA
C7G532
-
-
xylose (glucose) isomerase
-
-
xylose (glucose) isomerase
Streptomyces corchorusii J-59
-
;
-
xylose isomerase
-
-
xylose isomerase
Arthrobacter nicotianae BIM B-5
-
-
-
xylose isomerase
-
-
xylose isomerase
Escherichia coli DH5alpha, Escherichia coli HB101xylA
-
-
-
xylose isomerase
-
-
xylose isomerase
Lactococcus lactis 210 (Xyl-), Lactococcus lactis IO-1 (Xyl+)
-
-
-
xylose isomerase
no activity in Hansenula polymorpha
-
-
xylose isomerase
no activity in Hansenula polymorpha CBS4732s
-
-
-
xylose isomerase
no activity in Saccharomyces cerevisiae
-
-
xylose isomerase
Opuntia ficus-indica, Opuntia vulgaris
-
xylose isomerase exhibits two temperature stable isoforms having optimal activity at temperatures 70C (T70) and 90C (T90), respectively
xylose isomerase
-
-
xylose isomerase
Pectobacterium atrosepticum jn42xylA
-
-
-
xylose isomerase
-
-
xylose isomerase
-
-
xylose isomerase
-
-
xylose isomerase
-
-
xylose isomerase
-
-
xylose isomerase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-82-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Actinomyces olivocinereus
-
-
-
Manually annotated by BRENDA team
expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
Aerobacter levanicum
-
-
-
Manually annotated by BRENDA team
strain BIM B-5
-
-
Manually annotated by BRENDA team
Arthrobacter nicotianae BIM B-5
strain BIM B-5
-
-
Manually annotated by BRENDA team
Arthrobacter nicotianae BIM V-5
-
-
-
Manually annotated by BRENDA team
induced by presence of xylose and xylite. The synthesis of enzyme is controlled by catabolite repression occuring at the transcriptional level and mediated by cyclic 3',5'-AMP
-
-
Manually annotated by BRENDA team
strain HN-68
-
-
Manually annotated by BRENDA team
Bacillus coagulans HN-68
strain HN-68
-
-
Manually annotated by BRENDA team
No. KX-6
-
-
Manually annotated by BRENDA team
TX-3
-
-
Manually annotated by BRENDA team
Bacillus sp. No. KX-6
No. KX-6
-
-
Manually annotated by BRENDA team
Bacillus sp. TX-3
TX-3
-
-
Manually annotated by BRENDA team
Bacteroides stercoris HJ-15
-
-
-
Manually annotated by BRENDA team
Brevibacterium pentosoaminoacidicum
-
-
-
Manually annotated by BRENDA team
strain IPT101, gene xylA
Uniprot
Manually annotated by BRENDA team
Burkholderia sacchari IPT101
strain IPT101, gene xylA
Uniprot
Manually annotated by BRENDA team
recombinant enzyme from Hansenula polymorpha transformants
-
-
Manually annotated by BRENDA team
strain DH5alpha
-
-
Manually annotated by BRENDA team
strain HB101xylA
-
-
Manually annotated by BRENDA team
strain K-12
-
-
Manually annotated by BRENDA team
strain K-12, source of genes encoding xylose isomerase (xylA) and xylulokinase (xylB)
-
-
Manually annotated by BRENDA team
transformed strain LE392-pRK248/pTXI-1, that overproduces the enzyme by induction of the strong lambda PI promoter
-
-
Manually annotated by BRENDA team
Escherichia coli DH5alpha
strain DH5alpha
-
-
Manually annotated by BRENDA team
Escherichia coli HB101xylA
strain HB101xylA
-
-
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
Lactobacillus gayonii
-
-
-
Manually annotated by BRENDA team
Lactobacillus lycopersici
-
-
-
Manually annotated by BRENDA team
Lactobacillus mannitopoeus
-
-
-
Manually annotated by BRENDA team
strain 210 (Xyl-); strain IO-1 (Xyl+)
-
-
Manually annotated by BRENDA team
Lactococcus lactis 210 (Xyl-)
strain 210 (Xyl-)
-
-
Manually annotated by BRENDA team
Lactococcus lactis IO-1 (Xyl+)
strain IO-1 (Xyl+)
-
-
Manually annotated by BRENDA team
no activity in Corynebacterium glutamicum
-
-
-
Manually annotated by BRENDA team
no activity in Hansenula polymorpha
strain CBS4732s leu2-2
-
-
Manually annotated by BRENDA team
no activity in Hansenula polymorpha CBS4732s
strain CBS4732s leu2-2
-
-
Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
-
-
-
Manually annotated by BRENDA team
Opuntia vulgaris
-
-
-
Manually annotated by BRENDA team
Orpinomyces sp.
-
UniProt
Manually annotated by BRENDA team
Paracolobacterium aerogenoides
-
-
-
Manually annotated by BRENDA team
strain jn42xylA
-
-
Manually annotated by BRENDA team
Pectobacterium atrosepticum jn42xylA
strain jn42xylA
-
-
Manually annotated by BRENDA team
gene xylA
-
-
Manually annotated by BRENDA team
recombinant enzyme, expressed in Saccharomyces cerevisiae
-
-
Manually annotated by BRENDA team
source of xylose isomerase gene, a phylogenetic tree of the diversity of xylose isomerase genes is given - based on GenBank database
-
-
Manually annotated by BRENDA team
strain E2
-
-
Manually annotated by BRENDA team
designed strain TMB 3045, carrying the XI gene from Thermus thermophilus; strain TMB 3050, derived from strain TMB 3045, which carries the XI gene from Thermus thermophilus
-
-
Manually annotated by BRENDA team
Sarcina sp.
-
-
-
Manually annotated by BRENDA team
Streptococcus venuceus
-
-
-
Manually annotated by BRENDA team
NRRL 5778
-
-
Manually annotated by BRENDA team
Streptomyces albus NRRL 5778
NRRL 5778
-
-
Manually annotated by BRENDA team
recombinant enzyme from Hansenula polymorpha transformants
-
-
Manually annotated by BRENDA team
Streptomyces corchorusii J-59
strain J-59
-
-
Manually annotated by BRENDA team
Streptomyces diastaticus No. 7
strain M1033
-
-
Manually annotated by BRENDA team
Streptomyces diastaticus No. 7 M1033
strain M1033
-
-
Manually annotated by BRENDA team
Streptomyces nivens
-
-
-
Manually annotated by BRENDA team
NCIM 2730
-
-
Manually annotated by BRENDA team
thermophilic strain PLC
-
-
Manually annotated by BRENDA team
Streptomyces sp. NCIM 2730
NCIM 2730
-
-
Manually annotated by BRENDA team
Thermoanaerobacter ethanolicus JW200 (ATCC 31550)
-
UniProt
Manually annotated by BRENDA team
Thermoanaerobacterium saccharolyticum B6A-RI
B6A-RI
-
-
Manually annotated by BRENDA team
strain JW/SL-YS 489
-
-
Manually annotated by BRENDA team
Thermoanaerobacterium sp. JW/SL-YS 489
strain JW/SL-YS 489
-
-
Manually annotated by BRENDA team
Thermopolyspora sp.
-
-
-
Manually annotated by BRENDA team
Thermotoga neapolitana 5068
-
-
-
Manually annotated by BRENDA team
strain HB8
-
-
Manually annotated by BRENDA team
Thermus aquaticus HB8
strain HB8
-
-
Manually annotated by BRENDA team
source of xylose isomerase gene, a phylogenetic tree of the diversity of xylose isomerase genes is given - based on GenBank database
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
D2DK62, -
D-xylose isomerase is essential for xylose catabolism
metabolism
Thermoanaerobacter ethanolicus JW200 (ATCC 31550)
-
D-xylose isomerase is essential for xylose catabolism
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose
alpha-D-fructose
show the reaction diagram
-
-
-
-
r
D-Arabinose
?
show the reaction diagram
Thermus aquaticus, Thermus aquaticus HB8
-
-
-
-
-
D-D-glucose
D-fructose
show the reaction diagram
-
-
-
-
?
D-Fructose
?
show the reaction diagram
-
compulsory order of binding: 1. Co2+ binds first to site 2 and then to site 1, then the D-fructose binds at site 1. At normal concentrations Mg2+ binds at site 1, then D-fructose, and then Mg2+ at site 2. At very high Mg2+ concentrations, above 10 mM, the order is Mg2+ at site1, Mg2+ at site 2, then D-fructose
-
-
-
D-Fructose
?
show the reaction diagram
Thermoanaerobacterium saccharolyticum B6A-RI, Thermoanaerobacterium sp. JW/SL-YS 489
-
-
-
-
-
D-fructose
D-glucose
show the reaction diagram
-
-
-
-
r
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
r
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
r
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
r
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
P15587
-
-
-
r
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
P24300, -
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
r
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
r
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
P12851
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
r
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
r
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
r
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
C7G532
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
Opuntia vulgaris
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
-
no activity
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
-
with low efficiency
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
Thermotoga neapolitana 5068
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
Thermoanaerobacterium saccharolyticum B6A-RI
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
Streptomyces albus NRRL 5778
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
Bacillus coagulans HN-68
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
Thermoanaerobacterium sp. JW/SL-YS 489
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
Streptomyces corchorusii J-59
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
C7G532
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
Arthrobacter nicotianae BIM V-5
-
-
-
-
?
D-Glucose
D-Fructose
show the reaction diagram
Thermus aquaticus HB8
-
-
-
-
-
D-Glucose
D-Fructose
show the reaction diagram
Thermus aquaticus HB8
-
with low efficiency
-
-
-
D-glucose
?
show the reaction diagram
Escherichia coli, Arthrobacter nicotianae, Pectobacterium atrosepticum, Arthrobacter nicotianae BIM B-5, Escherichia coli HB101xylA, Pectobacterium atrosepticum jn42xylA
-
lower efficiency
-
-
?
D-Lyxose
?
show the reaction diagram
-
-
-
-
-
D-Ribose
D-Ribulose
show the reaction diagram
P12851
-
-
-
r
D-Ribose
?
show the reaction diagram
-
-
-
-
-
D-Ribose
?
show the reaction diagram
-
-
-
-
-
D-Ribose
?
show the reaction diagram
-
-
-
-
-
D-Ribose
?
show the reaction diagram
-
-
-
-
-
D-Ribose
?
show the reaction diagram
-
-
-
-
-
D-Ribose
?
show the reaction diagram
-
no activity
-
-
-
D-Ribose
?
show the reaction diagram
-
no activity
-
-
-
D-Ribose
?
show the reaction diagram
Streptomyces albus NRRL 5778
-
-
-
-
-
D-Ribose
?
show the reaction diagram
Bacillus coagulans HN-68
-
-
-
-
-
D-Ribose
?
show the reaction diagram
Arthrobacter nicotianae BIM B-5, Escherichia coli HB101xylA, Pectobacterium atrosepticum jn42xylA
-
weak effects
-
-
?
D-Ribose
?
show the reaction diagram
Thermus aquaticus HB8
-
-
-
-
-
D-ribose
L-arabinose
show the reaction diagram
P12851
-
-
-
r
D-Xylose
?
show the reaction diagram
Bacillus coagulans, Bacillus coagulans HN-68
-
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
P15587
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
P24300, -
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
P12851
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Actinomyces olivocinereus
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Streptomyces diastaticus No. 7
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
P26997
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
C7G532
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
D2DK62, -
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
Opuntia vulgaris
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
D-xylulose is an important intermediate in pentose metabolism
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
r
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
r
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
first step in xylose metabolism
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
first step of xylose metabolism
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
part of xylose metabolism
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
strain 3045 does not grow on xylose
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Streptomyces sp. NCIM 2730
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
Streptomyces sp. NCIM 2730
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
Thermotoga neapolitana 5068
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Thermoanaerobacterium saccharolyticum B6A-RI
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
Lactococcus lactis IO-1 (Xyl+)
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Thermoanaerobacter ethanolicus JW200 (ATCC 31550)
D2DK62
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Streptomyces albus NRRL 5778
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
Bacillus coagulans HN-68
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
Bacillus coagulans HN-68
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
Bacillus coagulans HN-68
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
Arthrobacter nicotianae BIM B-5, Escherichia coli HB101xylA
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
Thermoanaerobacterium sp. JW/SL-YS 489
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
Bacillus sp. No. KX-6
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
Lactococcus lactis 210 (Xyl-)
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Streptomyces corchorusii J-59
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Streptomyces diastaticus No. 7 M1033
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
Pectobacterium atrosepticum jn42xylA
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
Bacillus sp. TX-3
-
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
C7G532
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Arthrobacter nicotianae BIM V-5
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Thermus aquaticus HB8
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
Thermus aquaticus HB8
-
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
Bacteroides stercoris HJ-15
-
-
-
-
?
L-Arabinose
L-Ribulose
show the reaction diagram
-
-
-
-
?
L-Arabinose
L-Ribulose
show the reaction diagram
-
-
-
-
r
L-Arabinose
L-Ribulose
show the reaction diagram
P24300, -
low reaction efficiency
-
-
r
L-Arabinose
?
show the reaction diagram
-
-
-
-
-
L-Arabinose
?
show the reaction diagram
-
no activity
-
-
-
L-Arabinose
?
show the reaction diagram
-
no activity
-
-
-
L-Arabinose
?
show the reaction diagram
-
poor substrate
-
-
-
L-Arabinose
?
show the reaction diagram
Streptomyces albus NRRL 5778
-
-
-
-
-
L-Arabinose
?
show the reaction diagram
Arthrobacter nicotianae BIM B-5, Escherichia coli HB101xylA, Pectobacterium atrosepticum jn42xylA
-
weak effects
-
-
?
L-arabinose
D-ribose
show the reaction diagram
P12851
-
-
-
r
L-arabinose
D-ribulose
show the reaction diagram
P12851
-
-
-
r
L-Rhamnose
?
show the reaction diagram
Streptomyces albus, Streptomyces albus NRRL 5778
-
-
-
-
-
L-ribose
?
show the reaction diagram
-
no increased reaction rate observed for mutant F26W
-
-
?
L-ribose
L-ribulose
show the reaction diagram
P12851
-
-
-
?
additional information
?
-
-
important enzyme in degradation of xylans and metabolizing D-xylose via the pentose phosphate pathway
-
-
-
additional information
?
-
-
the recombinant enzyme catalyzes also the isomerization of D-glucose to D-fructose
-
-
-
additional information
?
-
Thermus aquaticus HB8
-
important enzyme in degradation of xylans and metabolizing D-xylose via the pentose phosphate pathway
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Glucose
D-Fructose
show the reaction diagram
Streptomyces corchorusii, Streptomyces corchorusii J-59
-
-
-
-
?
D-Xylose
?
show the reaction diagram
-
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
P15587
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
P24300, -
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
P12851
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Streptomyces diastaticus No. 7
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
P26997
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
D-xylulose is an important intermediate in pentose metabolism
-
?
D-Xylose
D-Xylulose
show the reaction diagram
-
first step in xylose metabolism
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
first step of xylose metabolism
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
part of xylose metabolism
-
r
D-Xylose
D-Xylulose
show the reaction diagram
Thermotoga neapolitana 5068
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Lactococcus lactis IO-1 (Xyl+)
-
-
-
-
?
D-Xylose
?
show the reaction diagram
Bacillus coagulans HN-68
-
-
-
-
-
D-Xylose
D-Xylulose
show the reaction diagram
Arthrobacter nicotianae BIM B-5, Escherichia coli HB101xylA
-
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
Lactococcus lactis 210 (Xyl-)
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Streptomyces corchorusii J-59
-
-
-
-
?
D-Xylose
D-Xylulose
show the reaction diagram
Streptomyces diastaticus No. 7 M1033
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
Pectobacterium atrosepticum jn42xylA
-
-
-
-
r
L-Arabinose
L-Ribulose
show the reaction diagram
-
-
-
-
?
additional information
?
-
Thermus aquaticus, Thermus aquaticus HB8
-
important enzyme in degradation of xylans and metabolizing D-xylose via the pentose phosphate pathway
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
most effectively activates D-glucose isomerization and D-ribose isomerization
Co2+
-
Co2+ is bound to the enzyme in a molar ratio of 4:1; required for D-glucose isomerization; the binding sites for Co2+ and Mn2+ are different from each other
Co2+
-
1.0 mM, partial activation, Km: 0.003 mM; the binding sites for Co2+ and Mn2+ are different from each other
Co2+
-
slight activation
Co2+
-
Mg2+ or Co2+ required for activity
Co2+
-
activates
Co2+
-
stimulates
Co2+
-
maximal activity in presence of both, 10 mM Mg2+ and 1 mM Co2+
Co2+
-
activates
Co2+
-
two metal ions bind per subunit to non-identical sites. Mg2+, Mn2+, and Co2+ are of comparable efficiency for the D-xylose isomerization. Co2+ is the most efficient cofactor for D-glucose isomerization
Co2+
-
Mg2+, Mn2+ or Co2+ required for maximal activity; when the metal ions are added separately the activation is 48-52%. The combination of Mg2+ and Co2+ results in activation of 83%. The combination of Mg2+ and Mn2+ or Co2+ and Mn2+ results in 58-59% activation
Co2+
-
less effective than Mg2+ in D-fructose isomerization
Co2+
-
Mg2+, Mn2+ or Co2+ required for maximal activity
Co2+
-
most effective activator of D-glucose isomerization
Co2+
-
less effective than Mg2+ in D-xylose isomerization
Co2+
Streptomyces diastaticus No. 7
-
rather than Mg2+
Co2+
-
required for activity
Co2+
-
XI is substantially structurally stabilized in the presence of CO2+
Co2+
-
depends on the origin of the enzyme
Co2+
-
can only partially substitute for Mg2+
Co2+
Opuntia ficus-indica, Opuntia vulgaris
-
purified T90 isoform, 100% activity at 10 mM Mn2+ plus 1 mM Co2+
Co2+
D2DK62, -
D-xylose and D-glucose isomerase activities of XylA are enhanced by Co2+. When 1 mM Co2+ and 10 mM Mg2+ are added together, the activity of XylA is increased by about 10% compared to 1 mM Co2+ only
Co2+
-
required for thermostability
Co2+
C7G532
59% activity compared to Mn2+
Co2+
-
the presence of Co2+ is associated with isozyme T80
Co2+
-
activates
Fe2+
-
slight activation
Fe2+
-
activates
Mg2+
-
activates D-glucose isomerization, D-xylose isomerization and D-ribose isomerization
Mg2+
-
1.0 mM, strong activation, Km: 0.03 mM; the binding sites for Co2+ and Mn2+ are different from each other
Mg2+
-
Co2+ or Mg2+ required for activity
Mg2+
-
activates, maximal activity at 10 mM
Mg2+
-
maximal activity in presence of both, 10 mM Mg2+ and 1 mM Co2+
Mg2+
-
activates
Mg2+
-
two metal ions bind per subunit to non-identical sites. Mg2+, Mn2+, and Co2+ are of comparable efficiency for the D-xylose isomerization
Mg2+
-
Mg2+, Mn2+ or Co2+ required for maximal activity; when the metal ions are added separately the activation is 48-52%. The combination of Mg2+ and Co2+ results in activation of 83%. The combination of Mg2+ and Mn2+ or Co2+ and Mn2+ results in 58-59% activation
Mg2+
-
best activator of D-fructose isomerization
Mg2+
-
Mg2+, Mn2+ or Co2+ required for maximal activity
Mg2+
-
activates D-glucose isomerization, D-xylose isomerization and D-ribose isomerization
Mg2+
-
most effective in activation of D-xylose isomerization
Mg2+
-
required for activity, most effective cation
Mg2+
-
XI is to a lesser extent structurally stabilized in the presence of Mg2+
Mg2+
-
depends on the origin of the enzyme
Mg2+
-
included in assay medium
Mg2+
-
stabilzes the enzyme
Mg2+
-
preferred metal ion, activates by 15-20%
Mg2+
D2DK62, -
D-xylose and D-glucose isomerase activities of XylA are enhanced by Mg2+
Mg2+
C7G532
recombinant XylA requires the addition of Mg2+ for optimum activity (100%)
Mg2+
-
activates
Mn2+
-
most effectively activates D-xylose isomerization
Mn2+
-
required for D-xylose isomerization; the binding sites for Co2+ and Mn2+ are different from each other
Mn2+
-
specifically required
Mn2+
-
activates
Mn2+
-
activates
Mn2+
-
two metal ions bind per subunit to non-identical sites. Mg2+, Mn2+, and Co2+ are of comparable efficiency for the D-xylose isomerization
Mn2+
-
Mg2+, Mn2+ or Co2+ required for maximal activity; when the metal ions are added separately the activation is 48-52%. The combination of Mg2+ and Co2+ results in activation of 83%. The combination of Mg2+ and Mn2+ or Co2+ and Mn2+ results in 58-59% activation
Mn2+
-
less effective than Mg2+ in activation of D-fructose isomerization
Mn2+
-
Mg2+, Mn2+ or Co2+ required for maximal activity
Mn2+
-
most effectively activates D-xylose isomerization
Mn2+
-
less effective than Mg2+ in activation of D-xylose isomerization
Mn2+
-
required for activity
Mn2+
P15587
essential for activity, there are two manganese atoms visible in the atomic resolution study
Mn2+
-
XI is substantially structurally stabilized in the presence of Mn2+
Mn2+
-
depends on the origin of the enzyme
Mn2+
Opuntia ficus-indica, Opuntia vulgaris
-
purified T90 isoform, 100% activity at 10 mM Mn2+ plus 1 mM Co2+
Mn2+
D2DK62, -
D-xylose isomerase activity of XylA is enhanced by Mn2+
Mn2+
-
required for thermostability
Mn2+
C7G532
41% activity compared to Mn2+
Mn2+
-
the presence of Mn2+ is associated with isozyme T80
Zn2+
-
weak cofactor for D-glucose isomerization
Zn2+
-
activates D-xylose isomerization
Mn2+
-
activates
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
additional information
C7G532
addition of Ca2+, Zn2+, Fe2+, or Cu2+ is not effective
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-O-Methyl-D-xylose
-
-
5-Thio-alpha-D-glucopyranose
-
competitive
8-hydroxyquinoline
-
above 5 mM
Ca2+
-
weak inhibition
Ca2+
-
strict competitive against Mg2+
Ca2+
-
no inhibitory effect
Ca2+
D2DK62, -
less than 10% residual activity for D-xylose and D-glucose isomerase activities of XylA at 1 mM Zn2+
Cu2+
-
strong inhibition
Cu2+
D2DK62, -
complete inhibition of D-xylose and D-glucose isomerase activities of XylA at 1 mM Cu2+
D-glucose
-
suppressed enzyme synthesis by increased D-glucose content from 0.1 to 1.5%, productivity maxima at 1.0%
D-glucose
-
suppressed enzyme synthesis by increased content from 0.1 to 1.5%, productivity maxima at 0.1%, if D-xylose is the carbon source: D-glucose supplementation suppresses formation of xylose isomerase
D-glucose
-
suppressed enzyme synthesis by increased D-glucose content from 0.1 to 1.5%, productivity maxima at 0.1% D-glucose, if D-xylose is the carbon source D-glucose supplementation suppresses formation of xylose isomerase
D-Mannitol
-
competitive
D-ribose
-
inhibits D-glucose isomerization
D-Sorbitol
-
competitive
D-Sorbitol
-
competitive against D-glucose, D-xylose, and D-ribose. Co2+ and Mg2+ prevent inhibition
D-Sorbitol
-
competitive
D-Sorbitol
-
-
D-Sorbitol
-
competitive
D-Sorbitol
-
-
D-Sorbitol
-
mixed-type inhibition
D-Threonohydroxamic acid
-
slow-binding competitive inhibitor with glucose as substrate
D-xylitol
-
competitive
D-xylitol
-
competitive
D-xylitol
-
competitive
D-xylose
-
inhibits D-glucose isomerization
D-xylose
-
0.13 mM, inhibits glucose isomerization
Dideoxyimino-D-glucitol
-
-
EDTA
-
no inactivation
EDTA
-
above 5 mM
EDTA
-
Mn2+, Mg2+, or Co2+ restore 60-70% of the original xylose isomerase activity
EDTA
-
complete inactivation in presence of Mg2+, Co2+ or Mn2+
EDTA
P15587
inactivates the enzyme
EDTA
D2DK62, -
less than 10% residual activity for D-xylose and D-glucose isomerase activities of XylA at 1 mM Zn2+
Fe2+
-
-
-
Fe2+
-
weak inhibition
-
Hg2+
-
no influence on activity
Ni2+
-
weak inhibition
PCMB
-
above 5 mM
Tris(hydroxymethyl)aminomethane
-
strong inhibition of D-glucose isomerization, slight inhibition of D-xylose isomerization, competitive
Tris(hydroxymethyl)aminomethane
-
-
xylitol
-
inhibits in vitro xylose isomerase activity severely and competitively
Zn2+
D2DK62, -
less than 10% residual activity for D-glucose isomerase activity and about 10% residual activity for D-xylose activity of XylA at 1 mM Zn2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
D-glucose
-
if D-xylose is the carbon source D-glucose supplementation stimulates formation of xylose isomerase
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
151
-
D-arabinose
-
-
50
-
D-fructose
-
D-xylose, mutant E181Q
110
-
D-fructose
-
with 10-400 mM Mg2+
170
-
D-fructose
-
30C
800
-
D-fructose
-
with 1-10 mM Mg2+
0.249
-
D-glucose
-
soluble enzyme
0.297
-
D-glucose
-
immobilized enzyme
29
-
D-glucose
-
-
52
-
D-glucose
-
60C, pH 7, mutant E372G/V379A
65.2
-
D-glucose
-
soluble wild type enzyme, at 80C, pH 7.0
86
-
D-glucose
-
-
86
-
D-glucose
-
D-lyxose, 30C
88.5
-
D-glucose
-
soluble wild type enzyme, at 90C, pH 7.0
90
-
D-glucose
-
-
121.5
-
D-glucose
-
immobilized CBD-TNX fusion protein, at 80C, pH 7.0
130
-
D-glucose
-
D-glucose, mutant enzyme His71Phe
130.8
-
D-glucose
-
60C, pH 7, mutant E372G/F163L
138
-
D-glucose
-
mutant enzyme His101Gln
142
-
D-glucose
-
-
142
-
D-glucose
-
glucose, wild-type enzyme
146.8
-
D-glucose
-
60C, pH 7, wild-type
148.9
-
D-glucose
-
immobilized CBD-TNX fusion protein, at 90C, pH 7.0
152
-
D-glucose
-
mutant enzyme His152Phe
157.8
-
D-glucose
-
unbound CBD-TNX fusion protein, at 80C, pH 7.0
160
-
D-glucose
-
60C, pH 7.3, with Co2+, wild-type
168
-
D-glucose
-
mutant enzyme His101Asn
171.8
-
D-glucose
-
60C, pH 7, mutant E372G
180
-
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, mutant D81A and wild-type
187
-
D-glucose
C7G532
in 50 mM sodium phosphate buffer (pH 7.5), at 40C
190
-
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, mutant D65A
198
-
D-glucose
-
mutant enzyme His101Asp
200
-
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q
210
-
D-glucose
-
60C
225
-
D-glucose
-
30C
230
-
D-glucose
-
-
244
-
D-glucose
P12851
mutant V135N
250
-
D-glucose
-
D-fructose, 60C
252
-
D-glucose
-
mutant enzyme His101Glu
259
-
D-glucose
-
-
259.6
-
D-glucose
Opuntia ficus-indica, Opuntia vulgaris
-
enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90C
288
-
D-glucose
-
-
290
-
D-glucose
-
wild-type enzyme
300
-
D-glucose
-
mutant D257N
310
-
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, mutants E221A and D56N
340
-
D-glucose
-
60C, pH 7.3, with Co2+, mutant E221A
400
-
D-glucose
-
-
400
-
D-glucose
-
D-glucose, mutant H220Q
500
-
D-glucose
-
mutant H220N
536.1
-
D-glucose
-
unbound CBD-TNX fusion protein, at 90C, pH 7.0
713
-
D-glucose
P12851
wild-type
920
-
D-glucose
-
-
1600
-
D-glucose
-
mutant F26W
1900
-
D-glucose
-
wild-type
2400
-
D-glucose
-
mutant E181D
5800
-
D-glucose
-
mutant D257E
77
-
D-ribose
-
-
145
-
D-ribose
-
-
190
-
D-ribose
-
30C
350
-
D-ribose
-
-
670
-
D-ribose
-
-
0.076
-
D-xylose
-
-
0.078
-
D-xylose
-
soluble enzyme
0.104
-
D-xylose
-
immobilized enzyme
1.1
-
D-xylose
-
-
2.25
-
D-xylose
-
wild-type
2.9
-
D-xylose
-
with 10 mM Mg2+
3.3
-
D-xylose
-
with 1 mM Co2+
3.3
-
D-xylose
-
D-xylose, with 30 mM Mg2+
3.3
-
D-xylose
-
D-xylose, 30C
3.44
-
D-xylose
-
60C, pH 7, wild-type
3.46
-
D-xylose
-
mutant R202M/Y218D/V275A
4.4
-
D-xylose
-
mutant S388T/K407E
4.8
-
D-xylose
-
wild-type enzyme
6.66
-
D-xylose
-
-
7
-
D-xylose
-
-
7.93
-
D-xylose
C7G532
in 50 mM sodium phosphate buffer (pH 7.5), at 40C
10
-
D-xylose
-
-
11
-
D-xylose
D2DK62, -
at 80C in 100 mM MOPS buffer, pH 7.0
11.7
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D/D375G
11.8
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D/K355A
15
-
D-xylose
-
-
15.2
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D
16
-
D-xylose
-
D-xylose, mutant H220Q
21.1
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D/D375G/V385A
25.1
-
D-xylose
-
60C, pH 7, mutant E372G/V379A
27.1
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D/V144A
28.7
-
D-xylose
-
60C, pH 7, mutant E372G
33
-
D-xylose
-
-
35
-
D-xylose
-
-
45
-
D-xylose
-
-
46.4
-
D-xylose
Opuntia ficus-indica, Opuntia vulgaris
-
enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90C
48
-
D-xylose
-
mutant D257E
49
-
D-xylose
-
mutant D257N
49.9
-
D-xylose
-
pH 7.5, recombinant enzyme
54.03
-
D-xylose
-
in 100 mM Tris-HCl buffer (pH 7.5), 10 mM MgCl2, at 30C
61.9
-
D-xylose
-
pH 7.5, native enzyme
66
-
D-xylose
-
mutant D255N
66
-
D-xylose
-
pH 7.5, recombinant enzyme
73
-
D-xylose
-
mutant E181D
89.4
-
D-xylose
-
60C, pH 7, mutant E372G/F163L
93
-
D-xylose
-
D-glucose
8
-
D-xylulose
-
-
153
-
L-arabinose
-
-
280
-
L-arabinose
-
30C
900
-
L-arabinose
-
mutant Q256D
1400
-
L-arabinose
-
mutant F26W
1500
-
L-arabinose
-
wild-type
312
-
L-rhamnose
-
-
438
-
L-ribose
P12851
mutant V135N
1312
-
L-ribose
P12851
wild-type
additional information
-
additional information
-
Km-value for D-xylose varies with the concentration Mn2+
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
Km-values for wild-type enzyme and mutants E186D and E186Q, activated by Mg2+, Mn2+ or Co2+
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3
-
D-arabinose
-
-
1.67
-
D-fructose
-
30C
20.5
-
D-fructose
-
60C
0.03
0.55
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, mutant E221A
0.031
0.51
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, mutant D56N
0.04
1.97
D-glucose
-
60C, pH 7.3, with Co2+, mutant E221A
0.2
-
D-glucose
-
mutant H220N
0.7
-
D-glucose
-
mutant H220Q
0.7
-
D-glucose
-
60C, pH 7, mutant E372G/F163L
0.833
-
D-glucose
-
60C, pH 7, wild-type
2.32
-
D-glucose
-
30C
3
6
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q; 60C, pH 7.3, with Mg2+ and Co2+, mutant D65A; 60C, pH 7.3, with Mg2+ and Co2+, mutant D81A
3.02
-
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q
3.23
-
D-glucose
-
-
3.3
-
D-glucose
-
60C, pH 7.3, with Co2+, wild-type; 60C, pH 7.3, with Mg2+ and Co2+, wild-type
3.37
-
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, mutant D65A
3.41
-
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, mutant D81A
3.47
-
D-glucose
P12851
mutant V135N
4.53
-
D-glucose
-
60C, pH 7.3, with Co2+, wild-type
4.54
-
D-glucose
C7G532
in 50 mM sodium phosphate buffer (pH 7.5), at 40C
5
-
D-glucose
-
mutant D257N
5.27
-
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, wild-type
6.99
-
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, mutant E221A
7.53
-
D-glucose
-
60C, pH 7.3, with Mg2+ and Co2+, mutant D56N
9.22
-
D-glucose
-
60C, pH 7.3, with Co2+, mutant E221A
9.3
-
D-glucose
-
mutant E181D
16.2
-
D-glucose
-
soluble wild type enzyme, at 80C, pH 7.0
16.3
-
D-glucose
-
60C, pH 7, wild-type
17.7
-
D-glucose
-
mutant D257E
19
-
D-glucose
-
soluble wild type enzyme, at 90C, pH 7.0
19.9
-
D-glucose
-
60C
20.5
-
D-glucose
-
mutant F26W
23.8
-
D-glucose
-
60C, pH 7, mutant E372G
24.9
-
D-glucose
-
wild-type enzyme
25.3
-
D-glucose
-
wild-type
26.3
-
D-glucose
P12851
wild-type
30.72
-
D-glucose
-
-
39.9
-
D-glucose
-
60C, pH 7, mutant E372G/V379A
50
-
D-glucose
-
-
63.3
-
D-glucose
-
unbound CBD-TNX fusion protein, at 80C, pH 7.0
66.9
-
D-glucose
-
60C, pH 7, mutant E372G/F163L
88.7
-
D-glucose
-
60C, pH 7, mutant E372G
96.3
-
D-glucose
-
immobilized CBD-TNX fusion protein, at 80C, pH 7.0
116
-
D-glucose
-
immobilized CBD-TNX fusion protein, at 90C, pH 7.0
172.6
-
D-glucose
-
unbound CBD-TNX fusion protein, at 90C, pH 7.0
0.0617
-
D-Lyxose
-
30C
0.515
-
D-ribose
-
30C
0.05
-
D-xylose
-
mutant H220N
0.08
-
D-xylose
-
mutant E217S
0.1
-
D-xylose
-
mutant E181Q
0.5
-
D-xylose
-
mutant D255N
0.6
-
D-xylose
-
mutant H220Q
0.9
-
D-xylose
-
mutant D257N
1.5
-
D-xylose
-
mutant E181D
2.8
-
D-xylose
-
with 1 mM Co2+
2.8
-
D-xylose
-
D-ribose
3.4
-
D-xylose
-
mutant D257E
4.15
-
D-xylose
-
with 10 mM Mg2+
8.6
-
D-xylose
-
-
8.88
-
D-xylose
-
30C
17.3
-
D-xylose
-
wild-type enzyme
46.6
-
D-xylose
-
60C, pH 7, wild-type
47
-
D-xylose
C7G532
in 50 mM sodium phosphate buffer (pH 7.5), at 40C
50.7
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D
61.65
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D/D375G/V385A
68.39
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D/D375G
70.8
-
D-xylose
-
60C, pH 7, mutant E372G/F163L
116
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D/K355A
124
-
D-xylose
-
mutant S388T/K407E
142
-
D-xylose
-
mutant R202M/Y218D/V275A
160.5
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D/V144A
184
-
D-xylose
-
wild-type
230
-
D-xylose
-
-
257.5
-
D-xylose
-
60C, pH 7, mutant E372G/V379A
258
-
D-xylose
-
60C, pH 7, mutant E372G/V379A
7.7
-
D-xylulose
-
-
0.1
-
L-arabinose
-
wild-type
0.155
-
L-arabinose
-
mutant F26W
0.158
-
L-arabinose
-
mutant Q256D
1.31
-
L-arabinose
-
30C
0.0226
-
L-ribose
P12851
mutant V135N
0.0252
-
L-ribose
P12851
wild-type
additional information
-
additional information
-
turnover numbers for wild-type enzyme and mutant enzymes E186D and E186Q, activated by Mg2+, Mn2+ or Co2+
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.024
-
D-glucose
C7G532
in 50 mM sodium phosphate buffer (pH 7.5), at 40C
9202
0.22
-
D-glucose
-
soluble wild type enzyme, at 90C, pH 7.0
9202
0.25
-
D-glucose
-
soluble wild type enzyme, at 80C, pH 7.0
9202
0.32
-
D-glucose
-
unbound CBD-TNX fusion protein, at 90C, pH 7.0
9202
0.4
-
D-glucose
-
unbound CBD-TNX fusion protein, at 80C, pH 7.0
9202
0.78
-
D-glucose
-
immobilized CBD-TNX fusion protein, at 90C, pH 7.0
9202
0.79
-
D-glucose
-
immobilized CBD-TNX fusion protein, at 80C, pH 7.0
9202
2.92
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D/D375G/V385A
9403
3.35
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D
9403
5.87
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D/D375G
9403
5.92
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D/V144A
9403
5.93
-
D-xylose
C7G532
in 50 mM sodium phosphate buffer (pH 7.5), at 40C
9403
9.8
-
D-xylose
P26997
pH 7.0, 60C, mutant N91D/K355A
9403
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.6
-
xylitol
-
60C, pH 7, wild-type
5.1
-
xylitol
-
in 100 mM Tris-HCl buffer (pH 7.5), 10 mM MgCl2, at 30C
33.2
-
xylitol
-
60C, pH 7, mutant E372G/V379A
68.7
-
xylitol
-
60C, pH 7, mutant E372G
1174
-
xylitol
-
60C, pH 7, mutant E372G/F163L
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00001
-
-
empty vector, carbon source: glucose; empty vector, expression analysis
0.00323
-
-
Escherichia coli K-12, control, expression analysis
0.006
-
-
with D-glucose as substrate
0.0076
-
-
native enzyme in cell extract
0.008
-
-
with D-glucose as substrate
0.00933
-
-
Pgap-xylA/xylB-Pgap-tal/tktA, expression analysis
0.00978
-
-
Pgap-xylA/xylB-Peno-tal/tktA, expression analysis
0.012
-
-
transformant delta-xyl1No.4(pEc)No.2b
0.013
-
-
transformant delta-xyl1No.4(pEc)No.2a
0.014
-
-
transformant delta-xyl1No.4(pScoel)No.4
0.015
-
-
transformant delta-xyl1No.4(pScoel)No.12
0.017
-
-
with D-xylose as substrate
0.017
-
-
Saccharomyces cerevisiae overexprssing five own enzymes of pentose phosphate pathway, deletion of an unspecific aldose reductase, overexpressing xylose isomerase from Piromyces sp., 30C
0.034
-
-
Pseudomonas putida S12 strain xylAB containing xylose isomerase and xylulokinase gene from Escherichia coli
0.0344
-
-
recombinant enzyme in yeast cell extract
0.04
-
-
Saccharomyces cerevisiae overexpressing xylose isomerase from Thermus thermophilus, 30C
0.042
-
-
+/-0.003, DELTAxyl1 DELTAxyl2-A(EcxylA) No. 1
0.0455
-
-
Pgap-xylA/xylB-Pgap-tal/tktA, carbon source: glucose
0.047
-
-
+/-0.003, DELTAxyl1 DELTAxyl2-A(EcxylA) No. 2
0.05
-
-
+/-0.004, DELTAxyl1 DELTAxyl2-A(EcxylA) No. 4L/3
0.065
-
-
Escherichia coli wild-type
0.0653
-
-
Pgap-xylA/xylB-Pgap-tal/tktA, carbon source: xylose
0.151
-
-
+/-0.009, DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA HpXYL3)
0.152
-
-
+/-0.009, DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA) No. 1
0.18
-
-
CRX1, grown on glucose, aerobic
0.188
-
-
+/-0.010, DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA) No. 2
0.209
-
-
+/-0.011, Escherichia coli, control strain
0.22
-
-
enzyme production in the presence of D-glucose
0.26
-
-
CRX1, grown on xylose, aerobic
0.27
-
-
CRX2, grown on xylose, anaerobic, aerobic-phase culture Xyl
0.29
-
-
CRX2, grown on glucose, anaerobic, aerobic-phase culture Xyl
0.3
-
-
CRX2, grown on xylose, anaerobic, aerobic-phase culture Glc
0.31
-
-
CRX2, grown on glucose, anaerobic, aerobic-phase culture Glc
0.35
-
-
CRX2, grown on glucose, aerobic
0.46
-
-
enzyme production in the presence of D-xylose
0.46
-
-
crude extract
0.47
-
-
enzyme production in the presence of D-xylose
0.6
-
-
recombinant enzyme
0.71
-
-
enzyme production in the presence of D-xylose
0.73
-
-
enzyme production in the presence of sucrose
0.81
-
-
enzyme production in the presence of D-glucose
0.82
-
-
+/-0.01, recombinant Saccharomyces cerevisiae strain TMB 3066
1
-
-
Saccharomyces cerevisiae overexpressing xylose isomerase from Thermus thermophilus, 85C
1.1
-
-
Saccharomyces cerevisiae overexprssing xylose isomerase from Piromyces sp., 30C; Saccharomyces cerevisiae strain CEN.PK overexprssing xylose isomerase (xylA gene) from Piromyces sp., TPI1 promoter, 30C
1.39
-
-
-
1.39
-
-
enzyme production in the presence of xylitol
1.46
-
B6VCW7, -
wild-type strain
1.63
-
-
crude extract
1.69
-
-
crude extract
2.2
-
-
purified recombinant enzyme
2.44
-
B6VCW7, -
recombinant overexpressing mutant strain
3
-
D2DK62, -
crude extract, at pH 7.0 and 85C
6.78
-
Opuntia ficus-indica, Opuntia vulgaris
-
enzyme isoform T90 from homogenate with xylose as a substrate, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90C
7.5
-
-
-
11.69
-
-
-
12.5
-
-
-
16.4
-
-
-
17
-
D2DK62, -
after 6fold purification, at pH 7.0 and 85C
204
-
-
pH 7.5, 70C
266.4
-
Opuntia ficus-indica, Opuntia vulgaris
-
enzyme isoform T90 after 39.2fold purification with xylose as a substrate, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90C
additional information
-
-
-
additional information
-
-
measurement of the degradation of xylose and glucose; measurement of the production of ethanol, glycerol, organic acids, xylitol, CO2; strains are cultivated under aerobic and anaerobic conditions
additional information
-
-
measurement of the degradation of xylose and glucose; measurement of the production of ethanol, glycerol, organic acids, xylitol, CO2; strain is cultivated under aerobic and anaerobic conditions
additional information
-
-
measurement of the degradation of xylose and glucose; measurement of the production of organic acids; strains are cultivated under aerobic and anaerobic conditions
additional information
-
-
measurement of ethanol production; measurement of the degradation of xylose, glucose and a xylose-glucose-mixture
additional information
-
-
measurement of xylose consumption and ethanol production; modification of established spectrophotometrical activity assay; no activity in: CBS 4732s leu2-2(control strain), DELTAxyl1, DELTAxyl1 DELTAxyl2-A, DELTAxyl1 DELTAxyl2-A DELTAxyl2-B
additional information
-
-
measurement of the consumption of xylose, mannose and glucose; measurement of the production of ethanol, glycerol and xylitol
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8.5
-
-
6
7
-
D-xylose, D-glucose, D-ribose
6
8
Opuntia ficus-indica, Opuntia vulgaris
-
purified T90 isoform
6.25
-
-
mutant E186Q, xylose isomerization, activated by Mn2+ or Mg2+
6.8
-
-
recombinant enzyme
7
10
-
-
7
-
-
D-glucose; D-ribose
7
-
P26997
assay at
7.3
-
-
wild-type enzyme, xylose isomerization, activated by Mg2+
7.5
-
-
-
7.5
-
-
assay at
7.5
-
Orpinomyces sp.
-
-
7.5
-
Opuntia ficus-indica, Opuntia vulgaris
-
purified T70 isoform
7.5
-
C7G532
-
7.9
-
-
wild-type enzyme, xylose isomerization, activated by Mg2+
7.9
-
-
-
8
8.2
-
in presence of Mg2+ and Co2+, mutants D65A and D163N/E167Q
8
8.5
-
D-xylose
8
8.5
-
D-fructose
8
-
-
-
8
-
-
in presence of Co2+, mutant E221A; in presence of Mg2+ and Co2+, mutants E221A and D56N
8.1
8.3
-
in presence of Mg2+ and Co2+, mutant D81A
8.5
-
-
in presence of Mg2+ and Co2+, wild-type
8.8
-
-
in presence of Co2+, wild-type
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
11
-
pH profile, overview
4
8.5
Opuntia ficus-indica, Opuntia vulgaris
-
the enzyme retains 60% of its activity even at pH 4.5
5
10
-
mutants E372G/V379A, E372G/F163L and E372G
5
8
-
wild-type
5
9
P26997
pH profiles of recombinant mutant enzymes, overview
5.5
9.5
-
pH 5.5: about 40% of maximal activity, pH 9.5: about 80% of maximal activity, D-fructose isomerization
6
10
-
pH 6: about 35% of maximal activity, pH 10: about 30% of maximal activity
6
10.5
-
about 75% of maximal activity at pH 6.0 and 10.5
6
11
-
pH 6: about 50% of maximal activity, pH 11: about 65% of maximal activity
6
11
C7G532
-
6
9
-
pH 6: about 70% of maximal activity, pH 9: about 90% of maximal activity
7
10
-
pH 7: about 40% of maximal activity, pH 10: about 13.5% of maximal activity
8
-
Orpinomyces sp.
-
42% residual activity
9
-
Orpinomyces sp.
-
complete loss of activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
37
-
Orpinomyces sp.
-
-
45
-
-
recombinant enzyme
60
-
-
-
60
-
-
and 80C
60
-
P26997
assay at
60
-
C7G532
-
70
-
-
soluble and immobilized enzyme
70
-
Opuntia ficus-indica, Opuntia vulgaris
-
purified T70 isoform
75
-
-
mutants E372G/V379A
78
-
-
D-glucose, activity increases up to 85C and remains constant nearly to 100C
80
85
-
at pH 6.5
80
85
-
-
80
-
-
and 60C
85
-
-
D-xylose,activity increases up to 85C and remains constant nearly to 100C
85
-
-
-
90
-
-
wild-type
90
-
Opuntia ficus-indica, Opuntia vulgaris
-
purified T90 isoform
95
-
-
mutants E372G/F163L and E372G
additional information
-
-
75-80C for mutant F26W
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
Opuntia ficus-indica, Opuntia vulgaris
-
the purified T90 isoform at pH 7.5 exhibits a preference to yield the forward isomerization reaction
25
85
-
temperature profile, overview
30
65
C7G532
-
30
70
-
30C: about 45% of maximal activity, 70C: about 10% of maximal activity
40
80
-
40C: about 40% of maximal activity, 80C, about 30% of maximal activity
40
90
P26997
temperature profiles of recombinant mutant enzymes, overview
50
70
-
50C: about 55% of maximal activity, 70C: about 65% of maximal activity
74
-
-
activity decreases dramatically above 74C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
Pseudomonas strain S12 containing xylose isomerase gene and xylulokinase gene from Escherichia coli strain DH5 alpha
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Arthrobacter sp. (strain NRRL B3728)
Erwinia carotovora subsp. atroseptica (strain SCRI 1043 / ATCC BAA-672)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42990
-
-
calculated from amino acid sequence
44000
-
-
SDS-PAGE, monomer
45000
-
-
SDS-PAGE
49000
-
-
SDS-PAGE
49700
-
-
calculated from amino acid sequence
50000
-
-
SDS-PAGE
68000
-
Opuntia ficus-indica, Opuntia vulgaris
-
purified T90 isoform, gel filtration
70000
73000
-
gel filtration
71000
-
Opuntia ficus-indica, Opuntia vulgaris
-
purified T70 isoform, gel filtration
96000
-
-
gel filtration
100000
-
-
gel filtration
108000
-
Orpinomyces sp.
-
PAGE
115000
117000
-
low speed sedimentation without reaching equilibrium, equilibrium sedimentation
120000
-
-
gel filtration
127000
-
-
equilibrium sedimentation
138000
140000
-
gel filtration, ultracentrifugal analysis
160000
-
-
gel filtration
160000
-
-
neutron diffraction
165000
-
-
equilibrium sedimentation
168000
-
-
gel filtration
171000
-
-
equilibrium sedimentation
180000
-
-
gel filtration
183000
-
-
gel filtration
183000
-
-
sucrose density gradient centrifugation
190000
-
C7G532
gel filtration
196000
-
-
gel filtration
197000
-
-
sucrose density gradient centrifugation
200000
-
-
gel filtration
210000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 66000, SDS-PAGE
?
D2DK62, -
x * 50000, SDS-PAGE
?
-
x * 68000, SDS-PAGE
?
Thermoanaerobacter ethanolicus JW200 (ATCC 31550)
-
x * 50000, SDS-PAGE
-
dimer
-
2 * 56000, SDS-PAGE
dimer
-
2 * 58000, SDS-PAGE
dimer
-
2 * 44000, SDS-PAGE
dimer
-
2 * 50000, the recombinant enzyme exists as homodimer and homotetramer, with the dimer being the more abundant form. The native enzyme exclusively exists as tetramer
dimer
-
2 * 50000, SDS-PAGE; 2 * 53620, calculation from cDNA deduced polypeptide sequence
dimer
Orpinomyces sp.
-
2 * 49000, SDS-PAGE
dimer
Bacillus sp. No. KX-6
-
2 * 58000, SDS-PAGE
-
homotetramer
Streptomyces diastaticus No. 7
-
alpha4, crystallization studies
homotetramer
-
alpha4, crystallization studies
homotetramer
C7G532
4 * 48000, SDS-PAGE; 4 * 49264, calculated from amino acid sequence
homotetramer
-
x-ray crystallography
homotetramer
Streptomyces diastaticus No. 7 M1033
-
alpha4, crystallization studies
-
homotetramer
-
4 * 48000, SDS-PAGE; 4 * 49264, calculated from amino acid sequence
-
monomer
-
1 * 130000, SDS-PAGE
monomer
Opuntia ficus-indica, Opuntia vulgaris
-
1 * 66000, SDS-PAGE
tetramer
-
or trimer, 4 * or 3 * 49000, SDS-PAGE
tetramer
-
4 * 43000, equilibrium sedimentation in 6 M guanidine HCl
tetramer
-
4 * 45000, SDS-PAGE
tetramer
-
4 * 43000, SDS-PAGE
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
-
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
4 * 50000, the recombinant enzyme exists as homodimer and homotetramer, with the dimer being the more abundant form. The native enzyme exclusively exists as tetramer
tetramer
-
4 * 47000, SDS-PAGE
tetramer
-
neutron diffraction
tetramer
-
alpha4, 4 * 44000, SDS-PAGE, gel filtration
tetramer
-
alpha4, crystal structure analysis
tetramer
Bacillus coagulans HN-68
-
or trimer, 4 * or 3 * 49000, SDS-PAGE
-
tetramer
Streptomyces corchorusii J-59
-
alpha4, 4 * 44000, SDS-PAGE, gel filtration
-
tetramer
Thermoanaerobacterium sp. JW/SL-YS 489, Thermus aquaticus HB8
-
4 * 50000, SDS-PAGE
-
trimer
-
or tetramer, 3 * or 4 * 49000, SDS-PAGE
trimer
-
3 * 53000, SDS-PAGE
trimer
-
3 * 50000, SDS-PAGE
trimer
-
3 * 45000, SDS-PAGE
trimer
Bacillus coagulans HN-68
-
or tetramer, 3 * or 4 * 49000, SDS-PAGE
-
trimer
Bacillus sp. TX-3
-
3 * 45000, SDS-PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no glycoprotein
-
-
no glycoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
crystal structure of complexes of D-xylose isomerase with deoxysugars
-
structures of the enzyme containing the inhibitors xylitol and D-sorbitol at 2.5 A and 2.3 A resolution respectively
-
wild-type and mutant enzymes
-
sitting drop vapour diffusion method at room temperature, space group 21212 with a: 87.976 A, b: 98.836 and c: 93.927 A
Streptomyces diastaticus No. 7
-
3.0 A crystal structure
-
D-threonohydroxamic acid soaked into the crystal, crystallographic structure at 1.6 A resolution
-
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
-
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
-
cooling crystallization from 0.17 M MgSO4 solution
-
neutron diffraction, largest crystals at 18C, 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
-
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
-
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
-
ammonium sulfate as precipitant, orthorhombic space group P212121 with a: 84.35 A, b: 123.6 A, c: 140.24 A
-
ortjorhombic space group P212121 with a: 84.35 A, b: 123.60 A and c: 140.24 A
-
at room temperature with polyethylene glycol 4000 as precipitant, orthorhombic space group P212121 with a: 73.34 A, b: 144.05 A and c 155.07 A
-
ortjorhombic space group P212121 with a: 73.34 A, b: 144.05 A and c: 155.07 A
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
50C, 60 min, complete inactivation below
4
-
-
room temperature, 30 min, stable above
4.5
-
-
50C, 60 min, 20% loss of activity
5
7
-
50C, 60 min, stable
5
9
-
soluble enzyme, stable
5
-
-
room temperature, 30 min, stable above
5.5
10
D2DK62, -
the enzyme is stable for 1 h from pH 5.5 to 10.0 at 60C
5.5
8.5
Opuntia ficus-indica, Opuntia vulgaris
-
the enzyme exhibits a broad range (5.5-8.5) of pH stability but denatures readily at pH values below 4.0
5.5
9
-
immobilized enzyme stable
6
11
-
40C, 30 min, stable
6
-
-
8C, 18 h, about 50% loss of activity
6.5
11
-
30C, 30 min
7
8
-
8C, 18 h, stable
7
8
-
70C for 1 h, 70-75% loss of activity at 80C
7
9
-
-
8
-
-
highest stability at, 60C, 30 min
9
-
-
50C, 60 min, 20% loss of activity
9
-
-
8C, 18 h, about 10% loss of activity
additional information
-
-
stable in acidic as well as basic pH in presence of divalent kations Mn2+, Co2+, and Mg2+
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
stable for more than 1 month
40
90
P26997
thermostability of recombinant mutant enzymes, overview
40
-
-
10 min, stable up to
45
-
-
purified recombinant enzyme, rapid inactivation
50
70
C7G532
the enzyme is stable up to 50C for 20 min. However, only 34% of the maximal activity is observed after preincubation at 60C for 20 min, and no activity is observed after preincubation at 70C for 20 min
50
80
-
30 min, in presence of Co2+, stable
50
-
-
1 h, stable
50
-
-
30 min, stable
50
-
-
pH 7.5, 30 min, stable up to
53
-
-
half life in presence of Co2+: 7 days, half-life in presence of Mg2+: 9 days, in presence of Mn2+ the enzyme activity remains constant for at least 10 days
60
-
-
30 days, stable in presence of 1 mM Co2+ or 10 mM Mg2+
60
-
-
pH 7.5, 30 min, about 35% loss of activity
60
-
-
10 min, 20% loss of activity
65
-
-
30 min, about 50% loss of activity
65
-
-
pH 6.5, stable for more than 5 h
65
-
-
mutant Q256D remains fully active for 60 min at 65C, whereas the activity is rapidly lost at 80C
65
-
-
purified recombinant enzyme, 1 h, complete inactivation
70
80
-
pH 7.8, 2 h, after following 2 h incubation at 80C 37.6% loss of activity, 70-75% loss of activity at 80C
70
-
-
30 min, about 70% loss of activity
70
-
-
about 65% loss of activity
70
-
-
10 min, stable up to
70
-
-
in presence of Mn2+, 50% loss of activity after 5 days
70
-
-
half-life in absence of divalent cations: 4 d. In presence of Mn2+ or Co2+ stable for at least 1 month
70
-
-
in the presence of CO2+, cell-free xylose isomerase retains 100% activity without loss of activity for 7 days
75
-
-
60 min, stable up to
75
-
-
wild-type enzyme remains fully active for 60 min at 75C
80
-
-
10 min, 80% loss of activity in absence of metal ions, 50% loss of activity in presence of 1 mM Mg2+, no loss of activity in presence of 1 mM Co2+
80
-
-
at least 10 min stable
80
-
-
mutant F26W remains fully active for 60 min at 80C
80
-
-
2 h leads to 30.5% loss of activity
80
-
-
2 h leads to 30.1% loss of activity
80
-
-
the melting temperature at xylose isomerase isoform T80 is at about 80C
82
-
-
half-life: 1 h
85
-
-
in the presence of CO2+, cell-free xylose isomerase retains 50% residual activity for 13.5 h
85
-
D2DK62, -
the enzyme has a half-life of 1 h at 85C
90
-
-
in the presence of CO2+, cell-free xylose isomerase retains 50% residual activity for 126 min
90
-
-
after 1 h incubation the recombinant and the wild-type enzymes retain 25 and 34% of their activity, respectively
90
-
Opuntia ficus-indica, Opuntia vulgaris
-
the melting temperature of the native enzyme isoform T90 is at 90C
97
112
-
chitin-binding domain-D-xylose isomerase fusion protein (CBD-TNXI) bound to chitin has a half-life approximately 3times longer than the soluble wild type xylose isomerase (19.9 h vs. 6.8 h, respectively). The unbound soluble CBD-TNXI has a significantly longer half-life (56.5 h) than the immobilized enzyme. TNXI-apo enzyme melts at 97.5C, while transitions at 100C and 112C are observed in the presence of Co2+ (0.5 mM) and Mn2+ (5.0 mM). The apo version of the immobilized enzyme melts at 104C, with transitions at 87C and 110C for the halo enzyme
98
-
-
half-life: 15 min
additional information
-
-
Mn2+, Co2+ and Ni2+ strongly protect the enzyme from heat denaturation
additional information
-
-
Co2+ is superior as protector against thermal inactivation at 80C
additional information
-
-
Mn2+ and Co2+ increase thermal stability
additional information
-
-
Tm: 50.3C (apoenzyme), 53.3C (in the presence of 5 microM Mg2+), 73.4C (in the presence of 5 microM Co2+), 73.6C (in the presence of 5 microM Mn2+)
additional information
-
-
Tm: 50.8C (apoenzyme), 56.2C (in the presence of 5 microM Mg2+), 56.2C (in the presence of 5 microM Co2+), 57.3C (in the presence of 5 microM Mn2+)
additional information
-
-
Tm: 64.1C (apoenzyme), 83.0C (in the presence of 5 microM Mg2+), 86.0C (in the presence of 5 microM Co2+), 86.1C (in the presence of 5 microM Mn2+)
additional information
-
-
Tm: 96.4C (apoenzyme), 97.6C (in the presence of 5 microM Mg2+), 97.5C (in the presence of 5 microM Co2+), 96.9C (in the presence of 5 microM Mn2+), 100.4C (in the presence of 5 mM Mg2+), 100.0C (in the presence of 5 mM Co2+), 100.5C (in the presence of 5 mM Mn2+), 100.9C (in the presence of 5 mM Ni2+), 100.5C (in the presence of 5 mM Ca2+), half-lives: 83.2 min in the presence of 2 mM Mn2+ at 99C, 6.9 min in the presence of 2 mM Mn2+ at 102C, 4.2 min in the presence of 2 mM Mn2+ at 104C, 2.3 min in the presence of 2 mM Mn2+ at 106C, 59.5 min in the presence of 2 mM Co2+ at 96C, 14 min in the presence of 2 mM Co2+ at 99C, 5.8 min in the presence of 2 mM Co2+ at 102C, 2.9 min in the presence of 2 mM Co2+ at 104C, 12 min in the presence of 2 mM Mg2+ at 92C, 2.3 min in the presence of 2 mM Mg2+ at 96C, 1.9 min in the presence of 2 mM Mg2+ at 99C, 1.3 min in the presence of 2 mM Mg2+ at 102C, 30 min in the absence of metal ions at 87C, 11.3 min in the absence of metal ions at 90C, 7.5 min in the presence of 5 mM Mg2+ and 0.5 mM Co2+ at 100C, 3.0 min in the presence of 0.5 mM Co2+ at 100C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glycinamidylated enzyme is less stable than the native enzyme in 8 M urea or on heating
-
Mn2+, Co2+ and Ni2+ strongly protect the enzyme from heat denaturation
-
Mg2+ and Co2+ protect from thermal denaturation
-
after operating at 70C for 5 days, the remaining enzyme activities of the immobilized enzyme and the whole cells in the presence of Mg2+ and Co2+ is 75%
-
Co2+ is superior as protector against thermal inactivation at 80C
-
Mn2+, Co2+, or Mg2+ required for thermal stability
-
immobilized enzyme remains stable for at least 45 d at 4C or at 25C, upon incubation at 70C the half-life is about 4 d
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acetone
-
70-80% of cross-linked crystalline xylose isomerase activity is left after incubation for 24 h at 50C 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 50C. Soluble xylose isomerase is considerably less stable in ethanol-containing solutions
Methanol
-
cross-linked crystalline xylose isomerase is inactivated in 24 h at 50C even more in maleate buffer containing 50% methanol
Pyridine
-
cross-linked crystalline xylose isomerase is inactivated in 24 h at 50C even more in maleate buffer containing 10% pyridine
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, pH 7.5, 5 mM MgSO4, stable for at least 6 months, in absence of Mg2+ loss of activity within 3 weeks
-
4C, stable for more than 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
one-step purification by high-performance immobilized copper-affinity chromatography
-
recombinant enzyme, by heat precipitation and cation exchange, proteins were 95% pure when estimated in SDS-PAGE
P12851
PAGE and SDS-PAGE, identical electrophoretic mobility of intact and denatured enzyme compared with xylose isomerase from Escherichia coli and Erwinia carotovora subsp. atroseptica
-
recombinant enzyme from Escherichia coli strain BL21(DE3)
-
PAGE and SDS-PAGE, identical electrophoretic mobility of intact and denatured enzyme compared with xylose isomerase from Arthrobacter nicotianae and Erwinia carotovora subsp. atroseptica
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by one-step affinity chromatography to over 90% purity
-
purified enzyme is insoluble and inactive; purified enzyme is soluble
-
ammonium sulfate precipitation, Dowex-1 anion exchange column chromatography, and Sephadex G-100 gel filtration
Opuntia ficus-indica, Opuntia vulgaris
-
PAGE and SDS-PAGE, identical electrophoretic mobility of intact and denatured enzyme compared with xylose isomerase from from Arthrobacter nicotianae and Escherichia coli
-
ammonium sulfate precipitation, Dowex-1 column chromatography, and Sephadex G-100 gel filtration
-
to homogeneity
-
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%
-
immunoaffinity purification
-
heat treatment and DEAE-Sepharose column chromatography
D2DK62, -
heat treatment, DEAE-Sepharose column chromatography and Q-Sepharose column chromatography
-
HiTrap Ni-chelating column chromatography
C7G532
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
wild-type and mutant enzymes, overexpression in Escherichia coli
-
expression in Escherichia coli
-
wild-type and mutant enzymes, expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli HB101
-
expressed in Saccharomyces cerevisiae
-
gene xylA, expression of the polyhydroxybutyrate producing enzyme in an enzyme-deficient knockout strain of Burkholderia sacchari restoring the ability of the cells to produce polyhydroxybutyrate and increasing cell growth, overview
B6VCW7, -
phylogenetic analysis, enzyme expression in Escherichia coli strain BL21(DE3)
-
phylogenetic analysis and enzyme sequence comparisons, functional expression of codon-optimized enzyme in Saccharomyces cerevisiae confers on the yeast cells the ability to metabolize D-xylose and to use it as the sole carbon and energy source. The recombinant enzyme shows reduced sensitivity to inhibition by xylitol
-
cloning and functional expression of enzymes from Escherichia coli in Pseudomonas putida; expression in Pseudomonas putida S12
-
co-overexpression of genes encoding xylose isomerase (EcxylA, Escherichia coli) and xylulokinase (XYL3, Hansenula polymorpha), expression of both genes is driven by Hansenula polymorpha GAP-DH promoter
-
Corynebacterium glutamicum is transformed with: xylose isomerase (xylA, Escherichia coli) and xylulokinase (xylB, Escherichia coli)-two recombinant strains of Corynebacterium glutamicum are obtained: CRX1 (xylA) and CRX2 (xylA/xylB)
-
expression in Escherichia coli JM105
-
expression in Hansenula polymorpha
-
expression in the yeast Hansenula polymorpha
-
transformants bearing the fused lac-xylA or tac-xylA gene, cloned into various high copy-number plasmids
-
Zymobacter palmae is transformed with: xylose isomerase (xylA, Escherichia coli), xylulokinase (xylB, Escherichia coli), transaldolase (tal, Escherichia coli), transketolase (tktA, Escherichia coli). Different promotors from Zymomonas mobilis ATCC 29191 are used: gap-dh (Pgap), enolase (Peno)
-
overexpression in Escherichia coli strain BL21(DE3) from vector pRAC
-
expression in Escherichia coli
-
expression in Saccharomyces cerevisiae
Orpinomyces sp.
-
expression in Saccharomyces cerevisiae
-
gene xylA, expression in Saccharomyces cerevisiae
-
phylogenetic analysis and enzyme sequence comparisons, functional expression of codon-optimized enzyme in Saccharomyces cerevisiae confers on the yeast cells the ability to metabolize D-xylose and to use it as the sole carbon and energy source. The recombinant enzyme shows reduced sensitivity to inhibition by xylitol
-
Saccharomyces cerevisiae is transformed with a gene encoding xylose isomerase originating from Piromyces sp.
-
xylose isomerase gene (Piromyces sp.) is overexpressed in Saccharomyces cerevisiae strain TMB3044 resulting in strain TMB 3066
-
expression in Escherichia coli (DH5-alpha) and Saccharomyces cerevisiae
-
gene XYL1, subcloning in Escherichia coli strain MC1061, functional expression in Corynebacterium glutamicum, ATCC13032. Biotransformation of xylose into xylitol appears to be influenced by xylose transport, which is in turn affected by the glucose concentration in the reaction medium
-
expression in the yeast Hansenula polymorpha
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli HB101
P15587
expression in Escherichia coli
-
expressed in Escherichia coli DH10B cells
D2DK62, -
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli HB101
-
expression in Escherichia coli or Bacillus subtilis
-
expression in Escherichia coli, sequence homology with enzymes from other sources
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in Escherichia coli BL21(DE3)
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli HB101
-
expression of mutant enzymes in Escherichia coli strain BL21 (DE3)
P26997
Saccharomyces cerevisiae is transformed with a gene encoding xylose isomerase (Thermus thermophilus)
-
expressed in Escherichia coli BL21(DE3) cells
C7G532
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
xylulose at a concentration of 0.005% (w/v) almost completely represses the xylose isomerase synthesis in Arthrobacter nicotianae
-
xylulose at a concentration of 0.005% (w/v) almost completely represses the xylose isomerase synthesis in Arthrobacter nicotianae
Arthrobacter nicotianae BIM V-5
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E186D
-
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
-
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
F26W
-
catalytic efficiency with L-arabinose is increased 2fold
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
-
catalytic efficiency with L-arabinose is increased 3fold, reaction rate with L-ribose is increased 6fold
V135N
P12851
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
D189L
-
the Glu140Lys and Asp189Lys mutant proteins are synthesized in the Escherichia coli host, but are incapable of folding correctly. Mutant Trp136Glu does not show any enzyme activity
E140L
-
the Glu140Lys and Asp189Lys mutant proteins are synthesized in the Escherichia coli host, but are incapable of folding correctly. Mutant Trp136Glu does not show any enzyme activity
DELTAxyl1
-
deficient in xylose reductase
DELTAxyl1 DELTAxyl2-A
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A
DELTAxyl1 DELTAxyl2-A (EcxylA) No. 1
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A, transformed with xylose isomerase xylA from Escherichia coli, strain 1
DELTAxyl1 DELTAxyl2-A (EcxylA) No. 2
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A, transformed with xylose isomerase xylA from Escherichia coli, strain 2
DELTAxyl1 DELTAxyl2-A (EcxylA) No. 4L/3
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A, transformed with xylose isomerase xylA from Escherichia coli, strain 4L/3
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA HpXYL3)
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B, transformed with xylose isomerase xylA from Escherichia coli and overexpressing endogenous xylulukinase xyl3
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA) No. 1
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B, transformed with xylose isomerase xylA from Escherichia coli, strain 1
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA) No. 2
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B, transformed with xylose isomerase xylA from Escherichia coli, strain 2
H101X
-
selective substitution of His101 or His271 shows that they are essential components of the active site
H271X
-
selective substitution of His101 or His271 shows that they are essential components of the active site
DELTAxyl1
Escherichia coli DH5alpha
-
deficient in xylose reductase
-
DELTAxyl1 DELTAxyl2-A
Escherichia coli DH5alpha
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A
-
DELTAxyl1 DELTAxyl2-A (EcxylA) No. 1
Escherichia coli DH5alpha
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A, transformed with xylose isomerase xylA from Escherichia coli, strain 1
-
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B
Escherichia coli DH5alpha
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B
-
E407K
-
2% of strain IO-1 wild-type activity
K407E
-
92% of wild-type activity
R202M
-
9% of strain IO-1 wild-type activity
R202M/V275A
-
26% of strain IO-1 wild-type activity
R202M/Y218D
-
9% of strain IO-1 wild-type activity
R202M/Y218D/V275A
-
62% of strain IO-1 wild-type activity and soluble
S247A
-
97% of wild-type activity
S247A/K407E
-
79% of wild-type activity
S247A/S388T
-
27% of wild-type activity
S388T
-
insoluble and 8% of wild-type activity
S388T/K407E
-
soluble and 50% of wild-type activity
T388S
-
11% of strain IO-1 wild-type activity
Y218D
-
14% of strain IO-1 wild-type activity
Y218D/V275A
-
24% of strain IO-1 wild-type activity
Y275A
-
24% of strain IO-1 wild-type activity
E407K
Lactococcus lactis 210 (Xyl-)
-
2% of strain IO-1 wild-type activity
-
R202M
Lactococcus lactis 210 (Xyl-)
-
9% of strain IO-1 wild-type activity
-
T388S
Lactococcus lactis 210 (Xyl-)
-
11% of strain IO-1 wild-type activity
-
Y218D
Lactococcus lactis 210 (Xyl-)
-
14% of strain IO-1 wild-type activity
-
Y275A
Lactococcus lactis 210 (Xyl-)
-
24% of strain IO-1 wild-type activity
-
E407K
Lactococcus lactis IO-1 (Xyl+)
-
2% of strain IO-1 wild-type activity
-
R202M
Lactococcus lactis IO-1 (Xyl+)
-
9% of strain IO-1 wild-type activity
-
T388S
Lactococcus lactis IO-1 (Xyl+)
-
11% of strain IO-1 wild-type activity
-
Y218D
Lactococcus lactis IO-1 (Xyl+)
-
14% of strain IO-1 wild-type activity
-
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
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
H101F
-
substitution of His101 by Phe completely abolishes enzyme activity. When His101 is changed to Glu, Gln, Asn, or Asp, approximately 10-16% of wild-type enzyme activity is retained by the mutant enzymes. The His101Gln mutant enzyme is resistant to diethyldicarbonate inhibition which completely inactivates the wild-type enzyme
W139A
-
replacement of W139 with F, M, or A results in increased catalytic efficience proportional to the decrease in hydrophobicity of the side chain of the substituted amino acid
W139F
-
replacement of W139 with F, M, or A results in increased catalytic efficience proportional to the decrease in hydrophobicity of the side chain of the substituted amino acid; the W139F substitution reduces the Km and increases the turnover number of the mutant towards glucose, while the reverse effect towards xylose is observed
W139F/V186S
-
double mutants, W139F/V186T and W139F/V186S have 5fold and 2fold higher catalytic efficiency, respectively, than does the wild-type
W139F/V186T
-
double mutants, W139F/V186T and W139F/V186S have 5fold and 2fold higher catalytic efficiency, respectively, than does the wild-type
W139M
-
replacement of W139 with F, M, or A results in increased catalytic efficience proportional to the decrease in hydrophobicity of the side chain of the substituted amino acid
D309K
-
no activity, Tm of 95.5C in the presence of 5 mM Mg2+ and 0.5 mM Co2+
E232K
-
no activity, Tm of 100.7C in the presence of 5 mM Mg2+ and 0.5 mM Co2+
E232K/D309K
-
no activity, Tm of 96.5C in the presence of 5 mM Mg2+ and 0.5 mM Co2+
E372G
-
broader pH range and nine times higher turnover for D-xylose at 60C than wild-type
E372G/F163L
-
broader pH range and nine times higher turnover for D-xylose at 60C than wild-type
N91D
P26997
site-directed mutagenesis
N91D
-
the mutant shows increased substrate specificity for D-xylose compared to the wild type enzyme
N91D/D375G
P26997
site-directed mutagenesis, the mutant shows increased activity but reduced thermostability compared to the wild-type enzyme
N91D/D375G/V385A
P26997
site-directed mutagenesis, the mutant shows increased activity but reduced thermostability compared to the wild-type enzyme
N91D/K355A
P26997
site-directed mutagenesis, the mutant shows increased activity but reduced thermostability compared to the wild-type enzyme
N91D/V144A
P26997
site-directed mutagenesis, the mutant shows increased activity but reduced thermostability compared to the wild-type enzyme
Y253C
-
a Tyr253 mutant in which a disulfide bridge is introduced at the A-B subunit interface shows reduced thermostability, that is identical in both oxidized and reduced forms and also reduced stability in urea. X-ray-crystallographic analysis of the Mn2+-xylitol form of oxidized Y253C shows a changed conformation of Glu185 and also alternative conformations for Asp254, which is a ligand to the site 2 metal ion. With fructose, Mg2+-Y253C has a similar Km to that of the wild-type, and its maximal velocity is also similar below pH 6.4, but declines thereafter. In presence of Co2+, Y253C has lower activity than wild-type at all pH values, but its activity also declines at alkaline pH
additional information
B6VCW7, -
overexpression of the polyhydroxybutyrate producing enzyme in an enzyme-deficient knockout strain of Burkholderia sacchari restoring the ability of the cells to produce polyhydroxybutyrate, overview. Expression in a wild-type strain does not lead to increased polyhydroxybutyrate repoduction and cell growth, overview
Hansenula polymorpha
-
yeast, strain CBS4732s leu2-2, deficient in beta-isopropyl malate dehydrogenase, deletions of genes encoding xylose reductase (xyl1) and xylitol dehydrogenases (xyl2-A and xyl2-B) - overexpression of xylA gene (Escherichia coli) and endogenous xyl3 gene
additional information
-
metabolic engineering of Corynebacterium glutamicum to broaden substrate utilization range
additional information
-
co-overexpression of xylose isomerase and endogenous xylulokinase in a Hansenula polymorpha strain lacking NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases activities. Recombinant strain displays improved ethanol production during the fermentation of xylose
Hansenula polymorpha
Escherichia coli DH5alpha
-
yeast, strain CBS4732s leu2-2, deficient in beta-isopropyl malate dehydrogenase, deletions of genes encoding xylose reductase (xyl1) and xylitol dehydrogenases (xyl2-A and xyl2-B) - overexpression of xylA gene (Escherichia coli) and endogenous xyl3 gene
-
additional information
Escherichia coli DH5alpha
-
co-overexpression of xylose isomerase and endogenous xylulokinase in a Hansenula polymorpha strain lacking NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases activities. Recombinant strain displays improved ethanol production during the fermentation of xylose
-
Y275A
Lactococcus lactis IO-1 (Xyl+)
-
24% of strain IO-1 wild-type activity
-
additional information
-
Saccharomyces cerevisiae: five enzymes of non-oxidative pentose-phosphate-pathway are induced, a unspecific aldose reductase is deleted
additional information
-
the overexpressing Saccharomyces cerevisiae strain RWB 218 shows sensitivity to inhibitor acetic acid, kinetics and stoichiometry, detailed overview. At pH 3.5 acetic acid had a strong and specific negative impact on xylose consumption rates, which, after glucose depletion, slowed down dramatically, leaving 50% of the xylose unused after 48 h of fermentation
additional information
-
establishing and optimization of ethanol production from hotcompressed water treatment of Japanese beech by bioconversion of D-xylose via xylose isomerase, production enhancement by process integration of saccharifi cation, isomerization, and fermentation, process schemes, overview
E372G/V379A
-
broader pH range and nine times higher turnover for D-xylose at 60C than wild-type
additional information
-
Saccharomyces cerevisiae: five enzymes of non-oxidative pentose-phosphate-pathway are induced, a non-specific aldose reductase is deleted
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
food industry
-
xylose isomerase is widely used for production of glucose fructose syrup, a natural sweetener in dietary and preventive nutrition
food industry
Arthrobacter nicotianae BIM V-5
-
xylose isomerase is widely used for production of glucose fructose syrup, a natural sweetener in dietary and preventive nutrition
-
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
synthesis
-
commercial importance in the production of high-fructose corn syrup, potential application in the production of ethanol from hemicelluloses
biotechnology
-
putative use of lignocellulosic biomass as feedstock for the chemical industry
energy production
-
bioethanol
energy production
-
genetic engineering of Zymobacter palmae in order to produce ethanol from xylose fermentation
energy production
-
genetic engineering of the yeast Hansenula polymorpha in order to increase ethanol production by D-xylose fermentation
synthesis
-
co-overexpression of xylose isomerase and endogenous xylulokinase in a Hansenula polymorpha strain lacking NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases activities. Recombinant strain displays improved ethanol production during the fermentation of xylose
synthesis
-
expression of Escherichia coli xylose isomerase and xylulokinase in Pseudomonas putida S12 for efficient utilization of D-xylose and L-arabinose. After laboratory evolution of strains by repeated transfer to fresh minimal medium with xylose, a strain that efficiently utilizes xylose at a considerably improved growth rate can be obtained. The high yield can be attributed in part to glucose dehydrogenase inactivity, whereas the improved growth rate may be connected to alterations in the primary metabolism. The evolved D-xylose-utilizing strain metabolizes L-arabinose as efficiently as D-xylose, while its ability to utilize glucose is not affected
energy production
Escherichia coli DH5alpha
-
genetic engineering of the yeast Hansenula polymorpha in order to increase ethanol production by D-xylose fermentation
-
synthesis
Escherichia coli DH5alpha
-
co-overexpression of xylose isomerase and endogenous xylulokinase in a Hansenula polymorpha strain lacking NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases activities. Recombinant strain displays improved ethanol production during the fermentation of xylose
-
food industry
Opuntia ficus-indica, Opuntia vulgaris
-
thermophilic xylose isomerase from Opuntia vulgaris can serve as a good alternate source of enzyme for use in the production of high fructose corn syrup
synthesis
Orpinomyces sp.
-
alcohol fermentation of xylose and mixed sugars by Saccharomyces cerevisiae constitutively overexpressing of the Orpinomyces sp. xylose isomerase, the Saccharomyces cerevisiae xylulokinase, and the Pichia stipitis SUT1 sugar transporter genes. A strain adapted for enhanced growth on xylose by serial transfer in xylose-containing minimal medium under aerobic conditions can ferment 20 g per l of xylose to ethanol with a yield of 0.37 g per g and production rate of 0.026 g per l and h. Raising the fermentation temperature from 30C to 35C results in a substantial increase in the ethanol yield and production as well as a significant reduction in the xylitol yield. Ethanol production from xylose and a mixture of glucose and xylose is achieved in complex medium containing yeast extract, peptone, and borate with a considerably high yield of 0.48 g per g
energy production
-
engineering Saccharomyces cerevisiae for alcoholic fermentation of D-xylose
energy production
-
genetic engineering of Saccharomyces cerevisiae in order to increase ethanol production by fermentation of D-xylose
synthesis
-
higher rates of xylose utilization by further improved strains make alcoholic fermentation of hemicellulose fractions of plant biomass a realistic enterprise
food industry
-
xylose isomerase isozyme T80 serves as potential alternate catalytic converter of glucose in the production of high-fructose corn syrup for the sweetener industry and for ethanol production
nutrition
-
industrial manufacture of high-fructose corn syrups
nutrition
Streptomyces corchorusii J-59
-
industrial manufacture 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
nutrition
-
high fructose corn syrups
synthesis
-
production of high fructose corn syrup
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
synthesis
-
commercial importance in the production of high-fructose corn syrup, potential application in the production of ethanol from hemicelluloses
energy production
-
engineering of Saccharomyces cerevisiae for alcoholic fermentation of D-xylose
synthesis
C7G532
the combination of TxyA, XloA, and XylA is useful tool for the D-xylulose production from beta-1,3-xylan
synthesis
-
the combination of TxyA, XloA, and XylA is useful tool for the D-xylulose production from beta-1,3-xylan
-