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Information on EC 3.2.1.24 - alpha-mannosidase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97UK5
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3.2.1.24 alpha-mannosidaseIUBMB Comments
Also hydrolyses alpha-D-lyxosides and heptopyranosides with the same configuration at C-2, C-3 and C-4 as mannose.
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Word Map
- 3.2.1.24
- oligosaccharide
- mannose
- glycosidases
-
n-linked
- swainsonine
- hydrolases
- mannans
- n-glycans
-
concanavalin
- alpha-fucosidase
- xylanase
- beta-n-acetylglucosaminidase
- beta-d-galactosidase
- beta-hexosaminidase
- cellulase
-
endo-beta-n-acetylglucosaminidase
-
high-mannose
- beta-d-glucosidase
- galactomannans
- 1-deoxymannojirimycin
-
asparagine-linked
-
jack
- beta-mannosidase
-
exoglycosidase
-
mannosylated
- man9glcnac2
- n-acetyl-beta-glucosaminidase
-
locust
- beta-d-glucuronidase
-
complex-type
- glucomannans
-
konjac
-
mannose-type
-
hemicellulases
- glc3man9glcnac2
- castanospermine
-
oligomannosides
- alpha-d-galactosidase
- alpha-d-glucosidase
-
mannose-rich
- beta-xylosidase
-
lipid-linked
- hexosaminidase
- beta-n-acetylhexosaminidase
-
mannose-containing
-
hybrid-type
- i-cell
- mucolipidosis
-
oligomannose
- analysis
- cellulosome
- diagnostics
- medicine
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
alpha-mannosidase, mannanase, alpha-d-mannosidase, lysosomal alpha-mannosidase, alpha-mannosidase ii, alpha1,2-mannosidase, golgi alpha-mannosidase ii, alpha-1,2-mannosidase, alpha-man, man2c1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,2-alpha-D-mannosidase
-
-
-
-
1,2-alpha-mannosidase
-
-
-
-
Alpha mannosidase 6A8B
-
-
-
-
alpha-D-mannopyranosidase
-
-
-
-
alpha-D-mannosidase
-
-
-
-
Alpha-D-mannoside mannohydrolase
-
-
-
-
AMAN
-
-
-
-
exo-alpha-mannosidase
-
-
-
-
Laman
-
-
-
-
Lysosomal acid alpha-mannosidase
-
-
-
-
p-nitrophenyl-alpha-mannosidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-mannoside mannohydrolase
Also hydrolyses alpha-D-lyxosides and heptopyranosides with the same configuration at C-2, C-3 and C-4 as mannose.
CAS REGISTRY NUMBER
COMMENTARY
9025-42-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc + H2O
alpha-D-mannose + ?
-
-
-
?
alpha-D-Man-(1->2)-D-Man + H2O
2 alpha-D-mannose
-
-
-
?
alpha-D-Man-(1->3)-D-Man + H2O
2 alpha-D-mannose
-
-
-
?
alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc + H2O
alpha-D-mannose + ?
-
-
-
?
alpha-D-Man-(1->6)-D-Man + H2O
2 alpha-D-mannose
-
-
-
?
RNase-B-Man(n)-glycoform + H2O
RNase-B-Man(n-1)-glycoform + alpha-D-mannose
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
no hydrolysis observed on 4-nitrophenyl alpha-D-glucoside, 4-nitrophenyl alpha-D-galactoside, 4-nitrophenyl alpha-D-xyloside, 4-nitrophenyl alpha-L-arabinoside, 4-nitrophenyl alpha-L-rhamnoside, 4-nitrophenyl alpha-L-fucoside, and 4-nitrophenyl beta-L-fucoside
-
-
?
additional information
?
-
the enzyme could be putatively involved in the turnover and/or the maturation of glycoprotein
-
-
?
additional information
?
-
-
the enzyme could be putatively involved in the turnover and/or the maturation of glycoprotein
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
the enzyme could be putatively involved in the turnover and/or the maturation of glycoprotein
-
-
?
additional information
?
-
-
the enzyme could be putatively involved in the turnover and/or the maturation of glycoprotein
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Co2+
Mn2+
Zn2+
additional information
Cd2+
with alpha-1,2-, alpha-1,3-, alpha-1,4-, or alpha-1,6-mannobiose as a substrate, Co2+ is the only metal ion promoting hydrolysis of all substrates. Mn2+, Cd2+, and Zn2+ can substitute to a varying extent
Cd2+
in the wild-type enzyme Cd2+ stimulates hydrolysis of 4-nitrophenyl alpha-D-mannoside to a 4fold lesser extent than Co2+. The side chains at positions 228 and 533 are involved in binding the activating metal ion as their primary function
Co2+
with alpha-1,2-, alpha-1,3-, alpha-1,4-, or alpha-1,6-mannobiose as a substrate, Co2+ is the only metal ion promoting hydrolysis of all substrates. Mn2+, Cd2+, and Zn2+ can substitute to a varying extent
Co2+
Co2+ is by far the most efficient metal ion in stimulating hydrolysis of 4-nitrophenyl alpha-D-mannoside. The side chains at positions 228 and 533 are involved in binding the activating metal ion as their primary function
Mn2+
with alpha-1,2-, alpha-1,3-, alpha-1,4-, or alpha-1,6-mannobiose as a substrate, Co2+ is the only metal ion promoting hydrolysis of all substrates. Mn2+, Cd2+, and Zn2+ can substitute to a varying extent
Mn2+
in the wild-type enzyme Mn2+ stimulates hydrolysis of 4-nitrophenyl alpha-D-mannoside to a 3.2fold lesser extent than Co2+. The side chains at positions 228 and 533 are involved in binding the activating metal ion as their primary function
Zn2+
the enzyme binds Zn2+ in vivo, it contains 2.9 Zn2+ per trimeric enzyme, corresponding to a single atom per subunit. 0.1 mM Zn2+ showes 2fold activation of recombinant enzyme
Zn2+
with alpha-1,2-, alpha-1,3-, alpha-1,4-, or alpha-1,6-mannobiose as a substrate, Co2+ is the only metal ion promoting hydrolysis of all substrates. Mn2+, Cd2+, and Zn2+ can substitute to a varying extent
Zn2+
in the wild-type enzyme Zn2+ stimulates hydrolysis of 4-nitrophenyl alpha-D-mannoside to a 3.6fold lesser extent than Co2+. The side chains at positions 228 and 533 are involved in binding the activating metal ion as their primary function
additional information
no change in the enzymatic activity is observed with Cu2+ or Ni2+ at 0.001-1 mM
additional information
-
no change in the enzymatic activity is observed with Cu2+ or Ni2+ at 0.001-1 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Zn2+
mutant enzymes H228Q, H533E, and H533Q, are all inhibited by high Zn2+ concentrations (1 mM)
swainsonine
the enzyme substituted with Zn2+ is considerably less sensitive to swainsonine compared with the Co2+-, Cd2+-, and Mn2+-substituted enzyme
additional information
activity is insensitive to 1-deoxymannojirimycin at concentration up to 2 mM. No change in the enzymatic activity is observed with 0.001-1 mM EDTA
-
additional information
-
activity is insensitive to 1-deoxymannojirimycin at concentration up to 2 mM. No change in the enzymatic activity is observed with 0.001-1 mM EDTA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.16
alpha-D-Man-(1->3)-D-Man
pH 5.0, 70°C, enzyme in complex with Co2+
2
alpha-D-Man-(1->6)-D-Man
pH 5.0, 70°C, enzyme in complex with Co2+
0.11
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, enzyme in complex with Co2+
0.13
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, mutant enzyme H533Q
0.35
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, wild-type enzyme
0.39
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, enzyme in complex with Mn2+
0.4
4-nitrophenyl alpha-D-mannoside
pH 6.5, 65°C, recombinant enzyme
0.45
4-nitrophenyl alpha-D-mannoside
pH 6.5, 65°C, native enzyme
0.47
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Mn2+, wild-type enzyme
0.65
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, enzyme in complex with Zn2+
0.7
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Mn2+, mutant enzyme H533Q
0.74
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, wild-type enzyme
0.99
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, enzyme in complex with Cd2+
1
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, untreated enzyme which with no externally added metal ion in the incubation assay
1.1
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 0.1 mM Zn2+, mutant enzyme H533Q
1.1
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Cd2+, mutant enzyme H533Q
1.1
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, mutant enzyme H228E
1.4
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, mutant enzyme H228E
1.7
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, mutant enzyme H228Q
1.9
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Cd2+, wild-type enzyme
1.9
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, mutant enzyme H533Q
2.5
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, mutant enzyme H228Q
2.7
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Cd2+, mutant enzyme H228E
2.9
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, mutant enzyme H533E
0.85
alpha-D-Man-(1->2)-D-Man
pH 5.0, 70°C, enzyme in complex with Co2+
2.3
alpha-D-Man-(1->2)-D-Man
pH 5.0, 70°C, enzyme in complex with Mn2+
2
alpha-D-Man-(1->4)-D-Man
pH 5.0, 70°C, enzyme in complex with Mn2+
2.5
alpha-D-Man-(1->4)-D-Man
pH 5.0, 70°C, enzyme in complex with Co2+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.9
alpha-D-Man-(1->3)-D-Man
pH 5.0, 70°C, enzyme in complex with Co2+
2
alpha-D-Man-(1->6)-D-Man
pH 5.0, 70°C, enzyme in complex with Co2+
0.088
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Mn2+, mutant enzyme H533Q
0.099
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, mutant enzyme H533Q
0.118
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, mutant enzyme H228E
0.4
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Cd2+, mutant enzyme H533Q
0.6
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, mutant enzyme H228Q
0.8
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, mutant enzyme H228E
1.18
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Cd2+, mutant enzyme H228E
1.42
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, mutant enzyme H533Q
1.6
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 0.1 mM Zn2+, mutant enzyme H533Q
1.6
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, mutant enzyme H228Q
4.3
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, mutant enzyme H533E
4.8
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, enzyme in complex with Mn2+
4.8
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Mn2+, wild-type enzyme
6.6
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, wild-type enzyme
10.5
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, untreated enzyme which with no externally added metal ion in the incubation assay
11.3
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, wild-type enzyme
12.5
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, enzyme in complex with Co2+
13.6
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, enzyme in complex with Zn2+
15.3
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Cd2+, wild-type enzyme
16.1
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, enzyme in complex with Cd2+
21
4-nitrophenyl alpha-D-mannoside
pH 6.5, 65°C, recombinant enzyme
158
4-nitrophenyl alpha-D-mannoside
pH 6.5, 65°C, native enzyme
3.1
alpha-D-Man-(1->2)-D-Man
pH 5.0, 70°C, enzyme in complex with Mn2+
5.5
alpha-D-Man-(1->2)-D-Man
pH 5.0, 70°C, enzyme in complex with Co2+
1.9
alpha-D-Man-(1->4)-D-Man
pH 5.0, 70°C, enzyme in complex with Mn2+
10.4
alpha-D-Man-(1->4)-D-Man
pH 5.0, 70°C, enzyme in complex with Co2+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
alpha-D-Man-(1->6)-D-Man
pH 5.0, 70°C, enzyme in complex with Co2+
0.014
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Mn2+, mutant enzyme H533E. KM is too high (above 10 mM for 4-nitrophenyl alpha-D-mannoside or.0.1 mM for Mn2+) to allow for determination of kinetic parameters other than kcat/KM
0.019
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Mn2+, mutant enzyme H228E. KM is too high (above 10 mM for 4-nitrophenyl alpha-D-mannoside or.0.1 mM for Mn2+) to allow for determination of kinetic parameters other than kcat/KM
0.038
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Mn2+, mutant enzyme H228Q. KM is too high (above 10 mM for 4-nitrophenyl alpha-D-mannoside or.0.1 mM for Mn2+) to allow for determination of kinetic parameters other than kcat/KM
0.046
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Cd2+, mutant enzyme H533E. KM is too high (above 10 mM for 4-nitrophenyl alpha-D-mannoside or.0.1 mM for Mn2+) to allow for determination of kinetic parameters other than kcat/KM
0.0732
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, mutant enzyme H533E. KM is too high (above 10 mM for 4-nitrophenyl alpha-D-mannoside or.0.1 mM for Mn2+) to allow for determination of kinetic parameters other than kcat/KM
0.11
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, mutant enzyme H228E
0.13
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Mn2+, mutant enzyme H533Q
0.24
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 0.1 mM Zn2+, mutant enzyme H533E. KM is too high (above 10 mM for 4-nitrophenyl alpha-D-mannoside or.0.1 mM for Mn2+) to allow for determination of kinetic parameters other than kcat/KM
0.24
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, mutant enzyme H228Q
0.36
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Cd2+, mutant enzyme H533Q
0.43
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Cd2+, mutant enzyme H228E
0.53
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Cd2+, mutant enzyme H228Q. KM is too high (above 10 mM for 4-nitrophenyl alpha-D-mannoside or.0.1 mM for Mn2+) to allow for determination of kinetic parameters other than kcat/KM
0.57
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, mutant enzyme H228E
0.75
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, mutant enzyme H533Q
0.76
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, mutant enzyme H533Q
0.94
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, mutant enzyme H228Q
1.5
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 0.1 mM Zn2+, mutant enzyme H533Q
1.5
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, mutant enzyme H533E
8.1
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Cd2+, wild-type enzyme
8.9
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Zn2+, wild-type enzyme
10.2
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Mn2+, wild-type enzyme
10.5
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, untreated enzyme which with no externally added metal ion in the incubation assay
12
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, enzyme in complex with Mn2+
16
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, enzyme in complex with Cd2+
21
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, enzyme in complex with Zn2+
32.3
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, 1 mM Co2+, wild-type enzyme
54
4-nitrophenyl alpha-D-mannoside
pH 6.5, 65°C, recombinant enzyme
120
4-nitrophenyl alpha-D-mannoside
pH 5.0, 70°C, enzyme in complex with Co2+
351
4-nitrophenyl alpha-D-mannoside
pH 6.5, 65°C, native enzyme
0.206
alpha-D-Man-(1->2)-D-Man
pH 5.0, 70°C, enzyme in complex with Zn2+
0.277
alpha-D-Man-(1->2)-D-Man
pH 5.0, 70°C, enzyme in complex with Cd2+
1.3
alpha-D-Man-(1->2)-D-Man
pH 5.0, 70°C, enzyme in complex with Mn2+
6.4
alpha-D-Man-(1->2)-D-Man
pH 5.0, 70°C, enzyme in complex with Co2+
0.102
alpha-D-Man-(1->3)-D-Man
pH 5.0, 70°C, enzyme in complex with Zn2+
0.185
alpha-D-Man-(1->3)-D-Man
pH 5.0, 70°C, enzyme in complex with Mn2+
0.28
alpha-D-Man-(1->3)-D-Man
pH 5.0, 70°C, enzyme in complex with Cd2+
4.2
alpha-D-Man-(1->3)-D-Man
pH 5.0, 70°C, enzyme in complex with Co2+
0.106
alpha-D-Man-(1->4)-D-Man
pH 5.0, 70°C, enzyme in complex with Zn2+
0.31
alpha-D-Man-(1->4)-D-Man
pH 5.0, 70°C, enzyme in complex with Cd2+
0.95
alpha-D-Man-(1->4)-D-Man
pH 5.0, 70°C, enzyme in complex with Mn2+
4.2
alpha-D-Man-(1->4)-D-Man
pH 5.0, 70°C, enzyme in complex with Co2+
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14.4
substrate: 4-nitrophenyl alpha-D-mannoside, pH 6.5, 65°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
wild-type enzyme and mutant enzymes H228E, H228Q, H533E, and H533Q
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2 - 6
pH 4.2: about 35% of maximal activity, pH 6.0: about 40% of maximal activity, wild-type enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
mutant PBL2025, that misses 50 genes (SSO3004-3050), including genes coding for a multitude of enzymes possibly involved in sugar degradation or metabolism, is complemented with one of the missing proteins, the alpha-mannosidase (SSO3006). The alpha-mannosidase complemented strain resembles the Sulfolobus solfataricus P2 behavior with respect to attachment of cells to glass and growth of cells in static biofilms. During expression of the alpha-mannosidase, glucose and mannose-containing extracellular polymeric substance levels changes in the recombinant strain during surface attachment and biofilm formation. alpha-Mannosidase might be involved in the modulation of the extracellular polymeric substance composition and/or in the de-mannosylation of the glycan tree, which is attached to extracellular glycosylated proteins in Sulfolobus solfataricus
physiological function
the enzyme could be putatively involved in the turnover and/or the maturation of glycoprotein
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D338G
inactive mutant enzyme. In presence of the external nucleophil (1 M) sodium formate the activity is partially rescued
D534A
mutant enzyme shows no detectable activity (kcat below 0.01 s-1) within the pH range of 3-7 and with Co2+ as the activating divalent metal ion
D534Q
mutant enzyme shows no detectable activity (kcat below 0.01 s-1) within the pH range of 3-7 and with Co2+ as the activating divalent metal ion
H228E/H533E
mutant enzyme shows no detectable activity (kcat below 0.01 s-1) within the pH range of 3-7 and with Co2+ as the activating divalent metal ion
H228Q
the mutant enzyme is inhibited at increasing Zn2+ concentrations. The catalytic rate is reduced for all enzymes compared to that of the wild-type enzyme, although less dramatically with some activating metal ions. The mutant enzyme has a structural integrity in terms of thermostability similar to that of the wild-type enzyme
H228Q/H533Q
mutant enzyme shows no detectable activity (kcat below 0.01 s-1) within the pH range of 3-7 and with Co2+ as the activating divalent metal ion
H533E
the mutant enzyme is inhibited at increasing Zn2+ concentrations. The catalytic rate is reduced for all enzymes compared to that of the wild-type enzyme, although less dramatically with some activating metal ions The mutant enzyme has a structural integrity in terms of thermostability similar to that of the wild-type enzyme
H533Q
the mutant enzyme is inhibited at increasing Zn2+ concentrations. The catalytic rate is reduced for all enzymes compared to that of the wild-type enzyme, although less dramatically with some activating metal ions The mutant enzyme has a structural integrity in terms of thermostability similar to that of the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a fusion of the glutathione S-transferase of Schistosoma japonicum in Escherichia coli
overexpression in Sulfolobus solfataricus mutant PBL2025, that misses 50 genes (SSO3004-3050), including genes coding for a multitude of enzymes possibly involved in sugar degradation or metabolism
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cobucci-Ponzano, B.; Conte, F.; Strazzulli, A.; Capasso, C.; Fiume, I.; Pocsfalvi, G.; Rossi, M.; Moracci, M.
The molecular characterization of a novel GH38 alpha-mannosidase from the crenarchaeon Sulfolobus solfataricus revealed its ability in de-mannosylating glycoproteins
Biochimie
92
1895-1907
2010
Saccharolobus solfataricus (Q97UK5), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97UK5)
Nielsen, J.W.; Poulsen, N.R.; Johnsson, A.; Winther, J.R.; Stipp, S.L.; Willemoes, M.
Metal-ion dependent catalytic properties of Sulfolobus solfataricus class ii alpha-mannosidase
Biochemistry
51
8039-8046
2012
Saccharolobus solfataricus (Q97UK5), Saccharolobus solfataricus P2 (Q97UK5)
Koerdt, A.; Jachlewski, S.; Ghosh, A.; Wingender, J.; Siebers, B.; Albers, S.V.
Complementation of Sulfolobus solfataricus PBL2025 with an alpha-mannosidase: effects on surface attachment and biofilm formation
Extremophiles
16
115-125
2012
Saccharolobus solfataricus (Q97UK5), Saccharolobus solfataricus P2 (Q97UK5)
Hansen, D.K.; Webb, H.; Nielsen, J.W.; Harris, P.; Winther, J.R.; Willemoes, M.
Mutational analysis of divalent metal ion binding in the active site of class II alpha-mannosidase from Sulfolobus solfataricus
Biochemistry
24
2032-2039
2015
Saccharolobus solfataricus (Q97UK5), Saccharolobus solfataricus P2 (Q97UK5)
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