We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
mannose isomerase, d-mannose isomerase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-mannose ketol-isomerase
-
-
-
D-Mannose isomerase
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-Mannose = D-fructose
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
intramolecular oxidoreduction
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-mannose aldose-ketose-isomerase
Also acts on D-lyxose and D-rhamnose.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-Rhamnose
D-Rhamnulose
-
-
-
?
D-fructose
D-mannose
-
the conversion of 25% D-fructose is 29.4% after 2h
-
?
D-fructose
D-mannose
AJH12524
-
-
r
D-fructose
D-mannose
-
-
r
D-fructose
D-mannose
-
-
-
r
D-fructose
D-mannose
-
-
r
D-Lyxose
?
-
-
-
?
D-Lyxose
D-Xylulose
-
-
-
?
D-Lyxose
D-Xylulose
-
-
-
?
D-Lyxose
D-Xylulose
-
-
-
?
D-Lyxose
D-Xylulose
-
-
-
?
D-Lyxose
D-Xylulose
-
-
-
?
D-Lyxose
D-Xylulose
reaction of EC 5.3.1.15
-
r
D-Lyxose
D-Xylulose
-
reaction of EC 5.3.1.15
-
r
D-Lyxose
D-Xylulose
reaction of EC 5.3.1.15
-
r
D-Mannose
?
-
-
-
?
D-Mannose
?
-
constitutive enzyme. Since the enzymes mannokinase and phosphomannose isomerase cannot be detected, the isomerase and an inducible fructokinase must have a function in the metabolism of mannose by this bacterium
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
AJH12524
-
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
r
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
-
-
?
D-Mannose
D-Fructose
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-fructose
D-mannose
-
the conversion of 25% D-fructose is 29.4% after 2h
-
-
?
D-Mannose
?
-
-
-
-
?
D-Mannose
?
-
constitutive enzyme. Since the enzymes mannokinase and phosphomannose isomerase cannot be detected, the isomerase and an inducible fructokinase must have a function in the metabolism of mannose by this bacterium
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Co2+
1 mM, 9.1fold activation
Ni2+
1 mM, 11.8fold activation
Fe2+
-
stimulates
Fe2+
1 mM, 2.1fold activation
Mn2+
-
stimulates
Mn2+
1 mM, 12.5fold activation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Al3+
-
2 mM, complete loss of activity
Ba2+
1 mM, 64% residual activity
Co2+
-
2 mM, partial loss of activity
D-mannitol
-
50 mM, slight inhibition
Fe2+
-
2 mM, complete loss of activity
Fe3+
-
2 mM, complete loss of activity
N-bromosuccinimide
-
partial inhibition at 0.1 mM, complete inhibition at 1 mM
phenylmethylsulfonyl fluoride
-
partial inhibition at 0.1 mM, complete inhibition at 1 mM
Cu2+
-
2 mM, complete loss of activity
Cu2+
1 mM, 16% residual activity
Hg2+
-
2 mM, complete loss of activity
Ni2+
-
2 mM, partial loss of activity
PCMB
-
partial inhibition at 0.1 mM, complete inhibition at 1 mM
PCMB
-
reversal by glutathione
Zn2+
-
2 mM, complete loss of activity
Zn2+
1 mM, 13% residual activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Chelating agents
-
activation
sulfhydryl compounds
-
activation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.1
D-fructose
-
-
27.3
D-fructose
pH 6.5, 65°C
203.7
D-fructose
AJH12524
pH 7.0, 45°C
15.5
D-Lyxose
pH 6.5, 65°C
1.4
D-mannose
-
-
20
D-mannose
-
pH 7.5, 35°C
32.8
D-mannose
pH 6.5, 65°C
86.4
D-mannose
AJH12524
pH 7.0, 45°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
51.8
D-Lyxose
pH 6.5, 65°C
17.2
D-fructose
pH 6.5, 65°C
27.7
D-fructose
AJH12524
pH 7.0, 45°C
40.9
D-mannose
AJH12524
pH 7.0, 45°C
94.8
D-mannose
pH 6.5, 65°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.35
D-Lyxose
pH 6.5, 65°C
0.136
D-fructose
AJH12524
pH 7.0, 45°C
0.63
D-fructose
pH 6.5, 65°C
0.473
D-mannose
AJH12524
pH 7.0, 45°C
2.88
D-mannose
pH 6.5, 65°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5 - 8
-
immobilized enzyme
7.5
-
-
7.5
-
mannose isomerization
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5 - 8
more than 50% of maximum activity
6 - 10.5
-
pH 6.0: about 65% of maximal activity, pH 10.5: about 50% of maximal activity
6 - 9.5
-
pH 6: about 35% of maximal activity, pH 9.5: about 40% of maximal activity
6.9 - 8.6
-
about 75% of maximal activity at pH 6.9 and 8.6
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
45
-
-
60
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
35 - 65
-
35°C: about 55% of maximal activity, 65°C: about 10% of maximal activity, 70°C: about 20% of maximal activity
40 - 68
-
40°C: about 45% of maximal activity, 68°C: about 25% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5.2
-
isoelectric focusing
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
cf. EC 5.3.1.15
UniProt
brenda
cf. EC 5.3.1.15
UniProt
brenda
-
AJH12524
GenBank
brenda
K12
-
-
brenda
-
-
-
brenda
mutant strain capable of growing with sucrose or fructose as carbon source
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
30% of the activity compared to mannose-grown cells
brenda
-
greatest enzyme activity
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A0A0S4P258_9BURK
402
0
46203
TrEMBL
-
A0A4U9Q8V9_STEMA
408
0
47443
TrEMBL
-
A0A238H7F3_9BURK
447
0
51054
TrEMBL
-
A0A653UL64_9BURK
409
0
47497
TrEMBL
-
A0A0D0G0W5_9BACI
109
1
12472
TrEMBL
-
A0A150K2B1_BACCO
136
0
15402
TrEMBL
-
A0A0A1F806_9BURK
409
0
47750
TrEMBL
-
R9PQJ9_AGAAL
394
0
45278
TrEMBL
-
A0A0D0FIJ2_9BACI
191
0
21931
TrEMBL
-
A0A0L0M9V3_9BURK
417
0
48086
TrEMBL
-
A0A3B0RQM4_9ZZZZ
402
0
46284
TrEMBL
other Location (Reliability: 5 )
A0A120AHF5_9GAMM
406
0
47219
TrEMBL
-
Q88P39_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
416
0
45472
TrEMBL
-
F9UQ52_LACPL
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
313
0
35210
TrEMBL
-
A0A3B0SL85_9ZZZZ
400
0
46636
TrEMBL
other Location (Reliability: 2 )
A0A4Y1ZB43_9BACL
408
0
47376
TrEMBL
-
A0A0L0M6B6_9BURK
399
0
46662
TrEMBL
-
A0A150K1W8_BACCO
252
0
29073
TrEMBL
-
A0A0J7JQJ0_9BURK
403
0
47061
TrEMBL
-
A0A655M3Z0_STEMA
408
0
47489
TrEMBL
-
A0A150JN78_BACCO
400
0
45856
TrEMBL
-
A0A0D0EUY3_9BACI
400
0
46150
TrEMBL
-
G4M4N0_9BURK
417
0
48309
TrEMBL
-
A0A3N6BK18_9BACI
399
0
46727
TrEMBL
-
A0A0L0M3X0_9BURK
408
0
47552
TrEMBL
-
F9UMZ8_LACPL
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
315
0
35272
TrEMBL
-
A0A0C5VQS2_9GAMM
392
0
46192
TrEMBL
-
F7PIL2_9EURY
396
0
45518
TrEMBL
-
A0A0A1FFA7_9BURK
406
0
46494
TrEMBL
-
F3BDR8_9GAMM
399
0
46949
TrEMBL
-
D9RZ53_THEOJ
Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 / JW/IW-1228P)
181
0
20841
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
274500
AJH12524
gel filtration
40000
-
4 * 40000, SDS-PAGE
44000
gel filtration
44000
-
2 * 44000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hexamer
AJH12524
6 * 45000, calculated from sequence, 6 * 45800, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
dimer
-
2 * 44000, SDS-PAGE
dimer
-
2 * 44000, SDS-PAGE
dimer
2 * 22000, SDS-PAGE
dimer
-
2 * 22000, SDS-PAGE
dimer
-
2 * 22000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
35
-
pH 7.5, 10 min, stable below
40
-
immobilized enzyme loses 46% of its activity after 4 d, soluble enzyme loses 45% of its activity after 4 d
50
-
pH 7.0, 10 min, stable
55
-
pH 7.5, 10 min, about 10% loss of activity
61.4
AJH12524
melting temperature
75
-
pH 7.0, 10 min, about 80% loss of activity
60
-
pH 7.5, 10 min, about 40% loss of activity
60
-
pH 7.0, 10 min, about 50% loss of activity
70
-
pH 7.5, 10 min, complete loss of activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
no loss of activity after 24 h dialysis against 50 mM Tris-HCl buffer containing 1 mM EDTA
-
stable in presence of 1 mM 2-mercaptoethanol or EDTA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
partial
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli BL21(DE3) cells
-
expression in Bacillus subtilis
AJH12524
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
synthesis
-
potential use of immobilized enzyme in a process for the production of fructose syrups containing a higher proportion of fructose
synthesis
AJH12524
expression in Bacillus subtilis leads to secretion of enzyme. Under optimum conditions, production of D-mannose using crude enzyme reaches about 150 g/l with approximately 25% turnover yield
synthesis
-
optimization of fermentation medium for producing intracellular D-mannose isomerase. The optimized medium containing 1.3% w/v D-mannose, and 0.055 % soybean meal results in 1.32fold enhanced D-mannose production of 1.638 Units/ml
synthesis
under optimum conditions, 101.6 g/l D-mannose is produced from 400 g/l D-fructose after reaction for 9 h, giving a conversion yield of 25.4%
synthesis
-
under optimum conditions, 101.6 g/l D-mannose is produced from 400 g/l D-fructose after reaction for 9 h, giving a conversion yield of 25.4%
synthesis
-
under optimum conditions, 101.6 g/l D-mannose is produced from 400 g/l D-fructose after reaction for 9 h, giving a conversion yield of 25.4%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Noltmann, E.A.
Aldose-ketose isomerases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
271-354
1972
Mycolicibacterium smegmatis, Lentzea aerocolonigenes, Pelomonas saccharophila, Acidovorax avenae, Acidovorax avenae S-48
-
brenda
Palleroni, N.J.; Doudoroff, M.
Mannose isomerase of Pseudomonas saccharophila
J. Biol. Chem.
218
535-548
1955
Pelomonas saccharophila
brenda
Hey-Ferguson, A.; Elbein, A.D.
Purification of a D-mannose isomerase from Mycobacterium smegmatis
J. Bacteriol.
101
777-780
1970
Mycolicibacterium smegmatis
brenda
Stevens, F.J.; Wu, T.T.
Growth on D-lyxose of a mutant strain of Escherichia coli K12 using a novel isomerase and enzymes related to D-xylose metabolism
J. Gen. Microbiol.
97
257-265
1976
Escherichia coli, Acidovorax avenae, Acidovorax avenae S-48
brenda
Stevens, F.J.; Stevens, P.W.; Hovis, J.G.; Wu, T.T.
Some properties of D-mannose isomerase from Escherichia coli K12
J. Gen. Microbiol.
124
219-223
1981
Escherichia coli
brenda
Allenza, P.; Morrell, M.J.; Detroy, R.W.
Conversion of mannose to fructose by immobilized mannose isomerase from Pseudomonas cepacia
Appl. Biochem. Biotechnol.
24-25
171-182
1990
Burkholderia cepacia
brenda
Sauerstein, J.; Ramm, M.; Schubert, K.; Reuter, G.
Nachweis einer direkten Isomerisierung von Mannose zu Fructose und ihre Bedeutung fur den Mannosestoffwechsel von Pseudomonas syringae pv. phaseolicola
J. Basic Microbiol.
28
673-679
1988
Pseudomonas savastanoi pv. phaseolicola
-
brenda
Takasaki, Y.; Hinoki, K.; Kataoka, Y.; Fukuyama, S.; Nishimura, N.; Hayashi, S.; Imada, K.
Enzymatic production of D-mannose from D-fructose by mannose isomerase
J. Ferment. Bioeng.
76
237-239
1993
Pseudomonas sp.
-
brenda
Hirose, J.; Maeda, K.; Yokoi, H.; Takasaki, Y.
Purification and characterization of mannose isomerase from Agrobacterium radiobacter M-1
Biosci. Biotechnol. Biochem.
65
658-661
2001
Agrobacterium tumefaciens, Agrobacterium tumefaciens M-1
brenda
Liu, Q.; Li, Q.; Yuan, Q.; Feng, W.
Expression of D-mannose isomerase in E. coli and a study of its catalytic activity
J. Beijing Univ. Chem. Technol.
38
101-104
2011
Agrobacterium tumefaciens
-
brenda
Siangsuepchart, A.; Lumyong, S.
Statistical optimization for the production of D-mannose isomerase by Saccharothrix sp. CMU-K747 using response surface methodology
Chiang Mai J. Sci.
42
52-62
2015
Saccharothrix sp. CMU-K747
-
brenda
Hu, X.; Zhang, P.; Miao, M.; Zhang, T.; Jiang, B.
Development of a recombinant D-mannose isomerase and its characterizations for D-mannose synthesis
Int. J. Biol. Macromol.
89
328-335
2016
Escherichia coli (AJH12524)
brenda
Yu, L.; Zhang, W.; Zhang, T.; Jiang, B.; Mu, W.
Efficient biotransformation of D-fructose to D-mannose by a thermostable D-lyxose isomerase from Thermosediminibacter oceani
Process Biochem.
51
2026-2033
2016
Thermosediminibacter oceani (D9RZ53), Thermosediminibacter oceani DSM 16646 (D9RZ53)
-
brenda
Select items on the left to see more content.
html completed