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3.2.1.24: alpha-mannosidase

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

Word Map on EC 3.2.1.24

Reaction

2-O-alpha-D-mannopyranosyl-D-mannopyranose
+
H2O
= 2 alpha-D-mannopyranose

Synonyms

1,2-alpha-D-mannosidase, 1,2-alpha-mannosidase, acid alpha-mannosidase, acidic alpha-mannosidase, alpha 1,2-mannosidase, Alpha mannosidase 6A8B, alpha-1,2-mannosidase, alpha-1,3 mannosidase, alpha-1,4 mannosidase, alpha-D-mannopyranosidase, alpha-D-mannosidase, Alpha-D-mannoside mannohydrolase, alpha-man, alpha-mann, alpha-mannosidase, alpha-mannosidase C, alpha-mannosidase E-II, alpha-mannosidase I, alpha-mannosidase IA, alpha-mannosidase II, alpha-mannosidase III, alpha1,2-mannosidase, AMAN, class II alpha-mannosidase, CpGH125, ER-alpha-mannosidase, ER-mannosidase II, exo-alpha-mannosidase, GH38 alpha-mannosidase, GH38 alpha-mannosidase II, GH38 class II alpha-mannosidase, GH38 enzyme, Golgi alpha-mannosidase II, Golgi mannosidase IA, Golgi mannosidase IB, Laman, Lysosomal acid alpha-mannosidase, lysosomal alpha-D-mannosidase, lysosomal alpha-mannosidase, Man1p, MAN2B1, Man2C1, Man2C1 alpha-mannosidase, ManA, mannanase, MGG_00994.6, More, neutral alpha-mannosidase, neutral/cytosol mannosidase, p-nitrophenyl-alpha-mannosidase, SpGH125, SpGH38, Ssa-man, SSO3006, TM1851, TMM, velmanase alfa

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.24 alpha-mannosidase

Engineering

Engineering on EC 3.2.1.24 - alpha-mannosidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D341N
-
the turnover numberis lower by roughly 200fold compared with that of wild-type enzyme
A95P
inactive
C501S
more than 30% of wild type activity
C501S/R950P
inactive
C55F
inactive
D149N
inactive
D74E
inactive
DELTAT887
T887SfsX45, c.2660delC causes a frameshift introducing a premature stop codon (p.T887SfsX45)
F1000S
inactive
G390C
inactive
G420V
inactive
G451C
20-30% of wild type activity
G800R
inactive
G800W
inactive
G891R
inactive
H200L
more than 30% of wild type activity
H200N
H445Y
inactive
L352P
inactive
L518P
missense mutantion c.1553 T
L565P
inactive
L809P
the mutation is associated with alpha-mannosidosis
L892P
inactive
L956R
inactive
P197R
inactive
P263L
inactive
P379L
20-30% of wild type activity
R202P
20-30% of wild type activity
R229W
20-30% of wild type activity
R750W
the mutation is associated with alpha-mannosidosis
R916C
inactive
R916H
inactive
R916S
missense mutantion c.2746 C>A, spatially close to the oldest known inherited alpha mannosidosis mutation p.R750W. Equal deleterious effect missense mutations indicating disease-causing mutations
R950P
inactive
S318L
more than 30% of wild type activity
S453F
20-30% of wild type activity
S453Y
inactive
T745R
inactive
V457E
more than 30% of wild type activity
Y99H
inactive
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
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
-
additional information
-
N-bromosuccinimide added to determine Trp-residues involved in enzyme activity. N-bromosuccinimide modified inactivation is monitored spectrophotometerically