Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.2.1.113: mannosyl-oligosaccharide 1,2-alpha-mannosidase

This is an abbreviated version!
For detailed information about mannosyl-oligosaccharide 1,2-alpha-mannosidase, go to the full flat file.

Word Map on EC 3.2.1.113

Reaction

Man6GlcNAc2-[protein] (isomer 6A1,2,3)
+
H2O
=
Man5GlcNAc2-[protein]
+
beta-D-mannopyranose

Synonyms

(alpha1,2)-mannosidase-I, 1,2-alpha-mannosidase, alpha-(1->2)-mannosidase I, alpha-1,2 mannosidase I, alpha-1,2-mannosidase, alpha-1,2-mannosidase IC, alpha-1,2-mannosidaseI, alpha-1-2-mannosidase, alpha-mannosidase, alpha1,2-mannosidase, alpha1,2-mannosidase I, alpha1-2-mannosidase I, At1g51590, At3g21160, class I endoplasmic reticulum 1,2-alpha-mannosidase, D2030.1, endoplasmic reticulum mannosidase I, ER alpha-1,2-mannosidase, ER-Man, exo-alpha-1,2-mannanase, FmanIBp, fungal alpha-1,2-mannosidase, glycoprotein processing mannosidase I, Golgi alpha-mannosidase I, Golgi alpha1,2-mannosidase I, Golgi alpha1,2-mannosidase IA, Golgi alpha1,2-mannosidase IB, Golgi alpha1,2-mannosidase IC, Golgi alpha1,2-mannosidase II, GolgiManI, HMIC, Man(9)-alpha-mannosidase, MAN1A1, MAN1A2, MAN1B1, MAN1C1, Man9 processing alpha-mannosidase, Man9-alpha-mannosidase, Man9-mannosidase, Man9GlcNAc2-specific processing alpha-mannosidase, manE, ManI, MANIa, ManIA2, MANIb, ManIC, mannose-9 processing alpha-mannosidase, mannosidase 1A, mannosidase 1B, mannosidase I, mannosidase, exo-1,2-alpha-, Mas1, MIa, MIa,b,c, MIb, MIc, MII, MIIx, MNS1, Mns1p, MNS2, msdC, N-glycan processing class I alpha-1,2-mannosidase, processing alpha-1,2-mannosidase IC

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.113 mannosyl-oligosaccharide 1,2-alpha-mannosidase

Engineering

Engineering on EC 3.2.1.113 - mannosyl-oligosaccharide 1,2-alpha-mannosidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C334A
-
Tm-value of mutant enzyme is 49.6°C compared to 55.8°C for the wild-type enzyme. Km-value is 2.4fold lower than wild-type value, turnover-number is 2.2fold lower than wild-type value
C363A
-
Tm-value of mutant enzyme is 49.6°C compared to 55.8°C for the wild-type enzyme. Km-value is 1.1fold higher than wild-type value, turnover-number is 1.1fold lower than wild-type value
C443A
-
Tm-value of mutant enzyme is 51.9°C compared to 55.8°C for the wild-type enzyme. Km-value is identical to wild-type value, turnover-number is 1.3fold lower than wild-type value
C443D
-
relative activity is less than 50% of wild-tzype activity
C443G
-
Tm-value of mutant enzyme is 50.2°C compared to 55.8°C for the wild-type enzyme
C443L
-
relative activity is less than 50% of wild-tzype activity
C443M
-
relative activity is less than 50% of wild-tzype activity
C443S
-
Tm-value of mutant enzyme is 50.0°C compared to 55.8°C for the wild-type enzyme
C443T
-
Tm-value of mutant enzyme is 52.8°C compared to 55.8°C for the wild-type enzyme
C443V
-
relative activity is less than 50% of wild-tzype activity
EP1130
-
enzyme expression reduced
EP1588
-
enzyme expression reduced
EP1628
-
enzyme expression reduced
EP982
-
enzyme expression reduced
D463N
the mutant shows 0.1% of wild type catalytic efficiency
D463N/E599Q
the mutant shows 0.0003% of wild type catalytic efficiency
E330Q
the mutant shows 3.5% of wild type catalytic efficiency
E330Q/E599Q
the mutant shows 0.006% of wild type catalytic efficiency
E599Q
the mutant shows 0.0005% of wild type catalytic efficiency
up
hepatitis B virus upregulates host expression of class I alpha-1,2-mannosidases via the PPARalpha pathway. Hepatitis B virus increases the expression of alpha-mannosidases both in vitro and in vivo via activation of the PPARalpha pathway by its envelope protein
F468L
-
naturally occuring mutation, retains enzymic activity but defective in secretion of enzyme
F592S
-
naturally occuring mutation, no enzymic activity
M411T
-
naturally occuring mutation, retains enzymic activity but defective in secretion of enzyme
additional information