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

BRENDA support

3.2.1.25: beta-mannosidase

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

Word Map on EC 3.2.1.25

Reaction

Manbeta1-4GlcNAcbeta(1-4)GlcNAcbeta-Asn
+
H2O
=
GlcNAc-(1-4)-beta-GlcNAc-Asn
 +
beta-D-mannopyranose

Synonyms

beta-D-mannosidase, beta-MAN, beta-mannosidase, beta-mannosidase 2A, beta-mannoside mannohydrolase, betaMANNOS1, BglB, CmMan5, CmMan5a, exo beta-mannanase, exo-beta-D-mannanase, GH2 beta-mannosidase, GM-1, GM-2, HvBII, Man2A, ManB, mannanase, mannase, mannosidase 5A, mannosidase, beta-, OT-1, PH0501, TM1624

ECTree

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

Engineering

Engineering on EC 3.2.1.25 - beta-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
E206G
-
complete loss of activity
E314G
-
complete loss of activity
D199A
-
low activity
E462A
-
low activity
E555A
-
low activity
E555Q
-
molecular modeling and electron densitiy studies of the Michaelis complex
N461A
Q646A
W198A
-
low activity
W198G
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand
W200A
-
low activity
W345A
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand
W395A
-
low activity
W645A
Y537A
E330A
-
mutant enzyme displays no activity against mannan or 4-nitrophenyl-beta-mannopyranoside
R641H
-
natural mutant identified in a patient with beta-mannosidisis. Patient is homozygous for the mutation, which leads to a residual activity of about 7% in the patient's leukocytes, 11% in lymphoblasts and 14% in plasma. Expression in transfected cells also results in 7% residual activity
D206N
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 11fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 60fold higher than that for 4-nitrophenyl beta-D-mannopyranoside
Q77R
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 2fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 1.1fold higher than that for 4-nitrophenyl beta-D-mannopyranoside
Q77R/D206N
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 8fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 1.4fold higher than that for 4-nitrophenyl beta-D-mannopyranoside
D206N
-
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 11fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 60fold higher than that for 4-nitrophenyl beta-D-mannopyranoside
-
Q77R
-
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 2fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 1.1fold higher than that for 4-nitrophenyl beta-D-mannopyranoside
-
Q77R/D206N
-
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 8fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 1.4fold higher than that for 4-nitrophenyl beta-D-mannopyranoside
-
D206N
catalytically active mutant enzyme, similar temperature optimum like wild-type enzyme. The high-catalytic turn-over rate by D206N for beta-glucosidase activity makes it a useful enzyme in cellulose degradation at high temperatures
D206Q
mutant enzyme shows less than 10% hydrolytic activity than the wild-type toward 4-nitrophenyl glycosides
E207S
no hydrolytic activity
E399S
no hydrolytic activity
Q77R
mutant enzyme shows less than 10% hydrolytic activity than the wild-type toward 4-nitrophenyl glycosides
additional information