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Information on EC 3.2.1.113 - mannosyl-oligosaccharide 1,2-alpha-mannosidase
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3.2.1.113 mannosyl-oligosaccharide 1,2-alpha-mannosidaseIUBMB Comments
Involved in the synthesis of glycoproteins.
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Word Map
- 3.2.1.113
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bipolar
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episode
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mood
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psychiatric
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psycho
- lithium
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schizophrenia
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antidepressant
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mental
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antipsychotic
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comorbidity
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anxiety
- valproate
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outpatient
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monotherapy
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placebo
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double-blind
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inpatient
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social
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psychopathology
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dsm-iv
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suicide
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remission
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clinician
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adolescent
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diagnoses
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anticonvulsant
- risperidone
- carbamazepine
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placebo-controlled
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psychosocial
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youth
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euthymic
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symptomatology
- lamotrigine
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electroconvulsive
- hamilton
- olanzapine
- quetiapine
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schizoaffective
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emotional
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neuroleptic
- medicine
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panic
- pharmacology
- delirium
- drug development
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subscale
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psychotropic
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extrapyramidal
- diagnostics
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treatment-emergent
- hallucinations
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phenomenology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
(alpha1,2)-mannosidase-I, 1,2-alpha-mannosidase, 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 E-I, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(alpha1,2)-mannosidase-I
-
-
-
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1,2-alpha-mannosidase
alpha-1,2 mannosidase I
alpha-1,2-mannosidase
alpha-1,2-mannosidase IC
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-
-
-
alpha-1,2-mannosidaseI
alpha-mannosidase
alpha1,2-mannosidase
D2030.1
endoplasmic reticulum mannosidase I
ER alpha-1,2-mannosidase
-
-
-
-
ER mannosidase I
ERManI
exo-alpha-1,2-mannanase
-
-
-
-
glycoprotein processing mannosidase I
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-
-
-
Golgi alpha1,2-mannosidase I
Golgi alpha1,2-mannosidase IA
Golgi alpha1,2-mannosidase IB
Golgi alpha1,2-mannosidase IC
HMIC
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-
-
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Man(9)-alpha-mannosidase
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-
-
-
Man1p
Man9-mannosidase
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-
-
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Man9GlcNAc2-specific processing alpha-mannosidase
-
-
-
-
ManI
MANIa
MANIb
mannose-9 processing alpha-mannosidase
-
-
-
-
mannosidase 1A
-
-
-
-
mannosidase 1B
-
-
-
-
mannosidase I
-
-
-
-
mannosidase, exo-1,2-alpha-
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-
-
-
Mas1
MGG_00994.6
N-glycan processing class I alpha-1,2-mannosidase
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-
-
-
processing alpha-1,2-mannosidase IC
-
-
-
-
additional information
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not identical with aryl-alpha-mannosidase
1,2-alpha-mannosidase
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-
-
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alpha-1,2-mannosidase
-
-
-
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Golgi alpha1,2-mannosidase IA
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
Golgi alpha1,2-mannosidase IB
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
mechanism: ordered equilibrium
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Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
model for substrate and conformer selectivity, mechanism, computational study
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Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
2-alpha-mannosyl-oligosaccharide alpha-D-mannohydrolase
Involved in the synthesis of glycoproteins.
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CAS REGISTRY NUMBER
COMMENTARY
9068-25-1
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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
(Glc)1(Man)9(GlcNAc)2 + H2O
? + D-mannose
-
removal of one alpha1,2-linked mannose
-
-
-
(Glc)3(Man)9(GlcNAc)2 + H2O
? + D-mannose
-
removal of one alpha1,2-linked mannose
-
-
-
(Manalpha(1-2))nManalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3)) Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-3)Manbeta1-4GlcNAc beta1-4GlcNAc + D-mannose
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside
4-methylumbelliferone + D-mannose
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MUaMan, fluorogenic substrate
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-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
high mannose chains of thyroglobulin and phytohemagglutinin-P + H2O
? + D-mannose
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thyroglobulin: 70% of alpha1,2-mannose residues accessible
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-
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Man-alpha-1,2-Man-alpha-O-CH3 + H2O
methyl alpha-D-mannopyranoside + D-mannose
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-
-
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Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + H2O
Manalpha(1-3)[Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + 4 D-mannose
-
-
-
-
-
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
-
-
-
-
-
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-3)[Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + 3 D-mannose
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 2 H2O
(Man)5GlcNAc + 2 D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + H2O
? + D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)6(GlcNAc)2 + D-mannose
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-hexapeptide + H2O
(Man)6(GlcNAc)2-hexapeptide + D-mannose
-
substrate specificity not influenced by peptide moiety, removes 3 mannose residues
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2))Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-peptide + H2O
(Man)5(GlcNAc)-peptide + D-mannose
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
? + D-mannose
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
? + D-mannose
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNA + H2O
? + D-mannose
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
? + D-mannose
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2 + D-mannose
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2-Asn + D-mannose
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn + H2O
? + D-mannose
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)4GlcNAc + (Man)3GlcNAc + D-mannose
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)4(GlcNAc)2 + (Man)3(GlcNAc)2 + D-mannose
Manalpha(1->2)Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + D-mannose
-
-
-
?
Manalpha(1->2)Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + D-mannose
-
-
-
?
Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + D-mannose
-
-
-
?
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + D-mannose
-
-
-
?
methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
? + D-mannose
-
-
-
?
methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside + H2O
? + D-mannose
Q3HYC1
used in a spectrophotometric assay
-
-
?
methyl-2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside + H2O
? + D-mannose
-
-
-
-
?
pyridylamino derivative of (Man)9(GlcNAc)2 + H2O
pyridylamino derivative of (Man)5(GlcNAc)2 + D-mannose
-
-
after 120 h incubation, via specific intermediates: overview
?
2-O-alpha-D-mannopyranosyl-D-mannose + H2O
D-mannose
-
i.e. alpha-D-Man-(1-2)-D-Man
-
-
?
alpha-1,2-linked mannotetraose + H2O
? + D-mannose
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
-
overexpression of each Golgi alpha1,2-mannosidase enhances alpha1-antitrypsin null degradation and trimming of its N-glycans to alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
overexpression of each Golgi alpha1,2-mannosidase enhances alpha1-antitrypsin null degradation and trimming of its N-glycans to alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
?
baker's yeast mannan + H2O
? + D-mannose
-
releases 9.2% of total mannose
-
-
?
baker's yeast mannan + H2O
? + D-mannose
-
alpha-1,2-linked side-chains
-
-
?
baker's yeast mannan + H2O
? + D-mannose
-
alpha-1,2-linked side-chains
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-3)[Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + 3 D-mannose
-
-
-
-
-
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-3)[Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + 3 D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
i.e. (Man)9GlcNAc, specific for alpha-1,2-linked mannose residues
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
i.e. (Man)9GlcNAc, specific for alpha-1,2-linked mannose residues
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
product is Man6GlcNAc
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
products are Man5-8GlcNAc, with Man6GlcNAc being major product
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
pyridylamine-tagged Man9GlcNAc2
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
first product is Man6GlcNAc, followed by slower conversion to Man5GlcNAc
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
-
-
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
first product is Man6GlcNAc, followed by slower conversion to Man5GlcNAc
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
and (Man)6GlcNAc
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
best substrate
-
-
-
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
i.e. (Man)9GlcNAc, specific for alpha-1,2-linked mannose residues
and (Man)6GlcNAc
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
the terminal mannose on the middle antenna appears to be the most susceptible residue
-
-
-
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
removes all 4 alpha1,2-linked mannosyl residues
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
and (Man)6GlcNAc
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
i.e. (Man)9GlcNAc, specific for alpha-1,2-linked mannose residues
and (Man)6GlcNAc
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
-
-
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
best substrate
-
-
-
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
-
-
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
mutant R273L
product of mutant R273L, product of wild type is Man8GlcNAc
-
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
product is Man6GlcNAc
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
after long-term incubation, (Man)7GlcNAc and (Man)6GlcNAc after 4 h, (Man)8GlcNAc, (Man)7GlcNAc, (Man)6GlcNAc and (Man)5GlcNAc after 12 h incubation
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
removes all 4 alpha1,2-linked mannosyl residues
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)6(GlcNAc)2 + D-mannose
-
highly active on alpha(1-2) linked mannooligosaccharides
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)6(GlcNAc)2 + D-mannose
-
removes 3 of the 4 alpha1,2-linked mannosyl residues
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)6(GlcNAc)2 + D-mannose
-
i.e. (Man)9(GlcNAc)2
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)6(GlcNAc)2 + D-mannose
-
enzyme from endoplasmic reticulum removes only 1 or 2 alpha1,2-linked mannose residues
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)6(GlcNAc)2 + D-mannose
-
removes 3 of the 4 alpha1,2-linked mannosyl residues
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)6(GlcNAc)2 + D-mannose
-
removes 3 of the 4 alpha1,2-linked mannosyl residues
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)6(GlcNAc)2 + D-mannose
-
highly active on alpha(1-2) linked mannooligosaccharides
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)6(GlcNAc)2 + D-mannose
-
intact chitobiose core affects Man9-mannosidase specificity: reduction or removal of terminal N-acetylglucosamine residue increases hydrolytic susceptibility of the fourth alpha1,2-mannosyl-linkage
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2))Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-peptide + H2O
(Man)5(GlcNAc)-peptide + D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2))Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-peptide + H2O
(Man)5(GlcNAc)-peptide + D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
? + D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
? + D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
? + D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
? + D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNA + H2O
? + D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNA + H2O
? + D-mannose
-
hydrolysis at 39% (mannosidase IB) or 67% (mannosidase IA) the rate of (Man)9GlcNAc hydrolysis
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNA + H2O
? + D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNA + H2O
? + D-mannose
-
hydrolysis at 39% (mannosidase IB) or 67% (mannosidase IA) the rate of (Man)9GlcNAc hydrolysis
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
? + D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
? + D-mannose
-
-
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2 + D-mannose
-
as in Taka-amylase A
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2 + D-mannose
-
pyridylamino derivative of Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-3)ManbetaGlcNAc2
i.e. pyridylamino derivative of (Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2 + D-mannose
-
preferred substrate
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2 + D-mannose
-
very poor substrate
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2-Asn + D-mannose
-
i.e. GPIV
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2-Asn + D-mannose
-
i.e. GPIV
major product formed, 3.5 mol mannose/mol GP IV per h, i.e. GPI
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn + H2O
? + D-mannose
-
-
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn + H2O
? + D-mannose
-
hydrolysis at 18-25% the rate of (Man)9GlcNAc hydrolysis
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn + H2O
? + D-mannose
-
hydrolysis at 18-25% the rate of (Man)9GlcNAc hydrolysis
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)4GlcNAc + (Man)3GlcNAc + D-mannose
-
without alpha1,2-linked mannose residues: poor substrate
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)4GlcNAc + (Man)3GlcNAc + D-mannose
-
without alpha1,2-linked mannose residues: poor substrate
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)4(GlcNAc)2 + (Man)3(GlcNAc)2 + D-mannose
-
i.e. Manalpha(1-2)Manalpha(1-2)Manalpha(1-3) (Manalpha(1-6))ManbetaGlcNAc-betaGlcNAc
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)4(GlcNAc)2 + (Man)3(GlcNAc)2 + D-mannose
-
without alpha-1,2-linked mannose residues: no substrate
-
-
-
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)4(GlcNAc)2 + (Man)3(GlcNAc)2 + D-mannose
-
i.e. Manalpha(1-2)Manalpha(1-2)Manalpha(1-3) (Manalpha(1-6))ManbetaGlcNAc-betaGlcNAc
-
?
p-nitrophenyl-alpha-D-mannoside + H2O
4-nitrophenol + D-mannose
-
mannosidase IB: poor substrate, mannosidase IA: no substrate
-
-
?
additional information
?
-
-
no substrate: 3-O-alpha- and 6-O-alpha-D-mannobioses
-
-
-
additional information
?
-
-
no activity with p-nitrophenyl-alpha-mannoside, Manalpha(1-3)Man-OMe or Manalpha(1-6)Man-OMe
-
-
-
additional information
?
-
-
no substrate: 1,2-alpha-D-mannobiitol
-
-
-
additional information
?
-
-
no substrate: 1,2-alpha-D-mannobiitol
-
-
-
additional information
?
-
-
little or no activity with 4-methylumbelliferyl-alpha-mannoside, aryl-alpha-D-mannosides
-
-
-
additional information
?
-
-
effect of the alpha-1,2-mannosidic linkage in the alpha-1,3-branch of Man6GlcNAc2 on enzyme activity
-
-
-
additional information
?
-
-
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
-
additional information
?
-
-
targets misfolded glycoproteins for dislocation into the cytosol and destruction by 26 S proteasomes
-
-
-
additional information
?
-
-
the enzyme does not hydrolyze alpha-D-Manp-(1-3)-D-Manp and alpha-D-Manp-(1-6)-D-Manp
-
-
-
additional information
?
-
-
the enzyme does not hydrolyze alpha-D-Manp-(1-3)-D-Manp and alpha-D-Manp-(1-6)-D-Manp
-
-
-
additional information
?
-
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
-
additional information
?
-
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
-
additional information
?
-
-
mannosidase IA and B are quite similar in substrate specificity
-
-
-
additional information
?
-
-
mannosidase IA and B are quite similar in substrate specificity
-
-
-
additional information
?
-
-
the Htm1p exomannosidase activity requires processing of the N-glycan by glucosidase I, glucosidase II, and mannosidase I
-
-
-
additional information
?
-
-
no substrate: 4-methylumbelliferyl-alpha-mannoside
-
-
-
additional information
?
-
-
no substrate: 4-methylumbelliferyl-alpha-mannoside
-
-
-
additional information
?
-
-
pig liver enzyme substrate specificity resembles that of calf liver enzyme
-
-
-
additional information
?
-
-
no hydrolysis of alpha1,6-linkages
-
-
-
additional information
?
-
-
more specific towards Man-alpha-1,2-bonds, but also hydrolysis of alpha-1,3- and of alpha-1,6-bonds
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 2 H2O
(Man)5GlcNAc + 2 D-mannose
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
-
-
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
and (Man)6GlcNAc
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
and (Man)6GlcNAc
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
-
-
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
-
-
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
-
-
-
?
additional information
?
-
-
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
-
additional information
?
-
-
targets misfolded glycoproteins for dislocation into the cytosol and destruction by 26 S proteasomes
-
-
-
additional information
?
-
P39098
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
-
additional information
?
-
P45700
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
divalent cations
Mg2+
Mn2+
Zn2+
additional information
Ca2+
-
required for activity, isozyme MANIa shows 450% relative activity at 15 mM Ca2+, isozyme MANIb shows 600% relative activity at 15 mM Ca2+
Ca2+
-
required for activity. Optimum concentration 1.5 mM or 15 mM. Isoform ManIC is stable in the absence of Ca2+, even though Ca2+ is also effective for activity; required for activity. Optimum concentration 15 mM. the activity of soform ManIA2 is significantly decreased after incubation at 30°C without Ca2+, which is about 30% compared with the activity of the enzyme after incubation at 5°C. The enzyme activity of ManIA2 increases with increasing Ca2+ concentration until 12 mM
Ca2+
the enzyme assumes an (alphaalpha)7 barrel structure with a Ca2+ ion coordinated at the bas of the barrel
Ca2+
-
requirement, protects from thermal inactivation, Km value 0.5 mM
Zn2+
-
the activity of isoform ManIC is 94% in the presence of 15 mM Zn2+ and 50% in the presence of 1.5 mM Zn2+ compared with that of the original solution
additional information
-
Co2+, Cu2+, Mg2+, Mn2+, and Zn2+ have no effect on activity
additional information
-
isoform ManIA2 shows no activity in the presence of Co2+, Mn2+, and Cu2+; isoform ManIC shows no activity in the presence of Co2+ and Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-Cyclohexyl-3-(2-morpholinyl-4-ethyl)carbodiimide/glycine methylester
-
-
2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
6-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
brefeldin A
-
known inhibitor of vesicle transport, ablated intracellular turnover of the radiolabeled molecules. Plus digestion with potato acid phosphatase implies that phosphorylation of ER mannosidase I is responsible for the altered electrophoretic mobility
D-mannonolactam amidrazone
-
mannosidase inhibitor, MDCK-cells: in vivo and in vitro
deoxymannojirimycin hydrochloride
Q3HYC1
inhibitor at a final concentration of 0.5 mM, reduces the activity by 80%
EGTA
-
ethylene glycol-bis(beta-aminoethylether)-N,N,N',N'-tetraacetic acid
Mannosyl-mannose disaccharide
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
-
methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside
analogue of the minimal disaccharide substrate mannobiose. Cocrystallization and mass spectrometry data suggest that when methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside is incubated with the mannosidase for long periods of time it is cleaved and that methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside behaves as a substrate
1-deoxymannojirimycin
-
isozyme MANIa shows 20% residual activity at 0.1 mM 1-deoxymannojirimycin, isozyme MANIb shows 45% residual activity at 0.1 mM 1-deoxymannojirimycin
1-deoxymannojirimycin
-
trimming is inhibited preferentially by 1-deoxymannojirimycin, inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
1-deoxymannojirimycin
-
mannose analogue, specific inhibitor of alpha1,2-mannosidase. Focus on the effect of blocking alpha-mannosidases I in human hepatocarcinoma 7721 cells concerning with endoplasmic reticulum stress. Observed that 1-deoxymannojirimycin can also be a radical stimulus in inducing endoplasmic reticulum stress
1-deoxymannojirimycin
-
mannose analog, in vivo and in vitro; reversible (not by Ca2+)
1-deoxymannojirimycin
-
mannose analog, in vivo and in vitro; rat liver enzyme
Chloroquine
-
lysosomotrophic amine capable of raising the pH of acidic intracellular compartments, added to the medium with weak inhibition
Chloroquine
-
lysosomotrophic amine capable of raising the pH of acidic intracellular compartments, effect on the intracellular fate of endogenous mouse ER mannosidase I
EDTA
-
isozyme MANIa shows 20% residual activity at 1 mM EDTA, isozyme MANIb shows 35% residual activity at 1 mM EDTA, isozyme MANIb activity in the presence of 1 mM EDTA is restored by the addition of Ca2+
EDTA
-
enzyme loses 96% activity after dialysis in 50 mM PIPES buffer, pH 6.0, containing 2 mM EDTA. Addition of 10 mM Ca2+ recovers activity to 100%, addition of 10 mM Mg2+ recovers activity to 43%
EDTA
-
complete inactivition, Zn2+ restores, Ca2+, Cd2+, Mg2+, Ni2+, Na+ or Cu2+ restore partly
kifunensine
-
inhibits Golgi alpha1,2-mannosidase. Addition of kifunensine completely inhibits mannose trimming from alpha1-antitrypsin null (Hong Kong) in mock transfected cells. Kifunensine inhibits alpha1-antitrypsin null (Hong Kong) degradation in cells co-transfected with the Golgi mannosidases
kifunensine
-
general membrane-permeable inhibitor of alpha-mannosidase activity
kifunensine
inhibits Golgi alpha1,2-mannosidase. Addition of kifunensine completely inhibits mannose trimming from alpha1-antitrypsin null (Hong Kong) in mock transfected cells. Kifunensine inhibits alpha1-antitrypsin null (Hong Kong)degradation in cells co-transfected with the Golgi mannosidases; inhibits Golgi alpha1,2-mannosidase. Addition of kifunensine completely inhibits mannose trimming from alpha1-antitrypsin null (Hong Kong) in mock transfected cells. Kifunensine inhibits alpha1-antitrypsin null (Hong Kong)degradation in cells co-transfected with the Golgi mannosidases
kifunensine
-
general membrane-permeable inhibitor of alpha-mannosidase activity, effect on the intracellular fate of endogenous mouse ER mannosidase I
lactacystin
-
irreversible inhibitor of multicatalytic proteasomes, only a minor effect on the disappearance of radiolabeled human ER mannosidase I
lactacystin
-
irreversible inhibitor of multicatalytic proteasomes, effect on the intracellular fate of endogenous mouse ER mannosidase I
leupeptin
-
lysosomal protease inhibitor, intracellular turnover of pulse-radiolabeled recombinant human ER mannosidase I is substantially inhibited
leupeptin
-
lysosomal protease inhibitor, effect on the intracellular fate of endogenous mouse ER mannosidase I
swainsonine
-
inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
additional information
not inhibitory: swainsonine; not inhibitory: swainsonine
-
additional information
not inhibitory: swainsonine; not inhibitory: swainsonine
-
additional information
-
no inhibition by 4-nitrophenyl-alpha-mannoside, mannitol, L-mannono-1,4-lactone, PMSF
-
additional information
-
staurosporine and genistein have an effect, tesing arrested intracellular turnover in response to selective inhibition of serine kinase activity
-
additional information
-
cycloheximide, protein synthesis inhibitor. After a 2 h treatment with the protein synthesis inhibitor cycloheximide, ER and Golgi labeling observed with ManI-GFP fusion remains unchanged, showing that the steady state localization of ManI-GFP is the Golgi and the ER
-
additional information
comparison with 1-deoxymannojirimycin and kifunensine
-
additional information
-
mannosidase IA and B are quite similar in response to inhibitors
-
additional information
-
no inhibition by swainsonine; no or little inhibition by N,N-dimethyl-1-deoxymannojirimycin
-
additional information
-
no inhibition by mannose, alpha1,6-linked mannose oligosaccharide, castanospermine, deoxynojirimycin, 2,5-dihydroxymethyl-3,4-dihydroxypyrrolidine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphatidylcholine
-
activation, with acyl-chains of different lengths, above C-4
phosphatidylethanolamine
-
activation, in the presence of 3.5 mM Triton X-100
Zwitterionic phospholipids
-
activation, required for solubilized and purified enzyme, independent of acyl chain length or degree of saturation, an ordered lipid structure of either micelles or bilayers, mixed micelles together with Triton X-100
-
additional information
-
no activation by negatively charged phospholipids, dibutyryl-phosphocholine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
4-methylumbelliferyl-alpha-D-mannopyranoside
-
MUaMan, fluorogenic substrate. Vmax 36.2 nmol of 4-methylumbelliferone min-1 mg-1 of protein
0.015 - 0.51
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
0.068 - 0.26
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
0.6
methyl-2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
-
37°C, pH 6.0
additional information
additional information
-
kinetic constants of various substrate derivatives
-
0.719
Manalpha(1,2)Man-O-Me
-
pH 5.0, 30°C, mutant enzyme C443A; pH 5.0, 30°C, wild-type enzyme
0.015
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.5, mutant enzyme T688A
0.068
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 5.3, mutant enzyme E330Q
0.11
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 7.0, wild-type enzyme
0.12
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.8, mutant enzyme F659A
0.33
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.5, mutant enzyme R461L
0.47
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.5, mutant enzyme R597A
0.51
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.5, mutant enzyme R461A
0.068
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 5.3, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q
0.09
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q
0.11
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.8, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N; 37°C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, wild-type enzyme
0.15
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q/E599Q
0.16
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.7, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E599Q
0.21
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.9, pyridylamine-tagged Man9GlcNAc2, mutant enzyme H524A
0.26
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N/E599Q
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03 - 3.7
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
0.000026 - 3.7
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
0.03
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.8, mutant enzyme F659A
0.06
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.5, mutant enzyme T688A
0.07
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.5, mutant enzyme R461L
0.084
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 5.3, mutant enzyme E330Q
0.11
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.5, mutant enzyme R597A
0.6
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.5, mutant enzyme R461A
3.7
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 7.0, wild-type enzyme
0.000026
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.7, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E599Q
0.000027
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N/E599Q
0.00028
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q/E599Q
0.0046
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.8, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N
0.018
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q
0.084
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 5.3, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q
0.86
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 6.9, pyridylamine-tagged Man9GlcNAc2, mutant enzyme H524A
3.7
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37°C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
1-deoxymmanojirimycin
Candida albicans
-
inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
-
0.55
swainsonine
Candida albicans
-
inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
0.03
1-deoxymannojirimycin
Arabidopsis thaliana
Q8H116, Q9C512
37°C, pH 6.0, substrate methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
0.04
1-deoxymannojirimycin
Arabidopsis thaliana
Q8H116, Q9C512
37°C, pH 6.0, substrate methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
0.00035
kifunensine
Arabidopsis thaliana
Q8H116, Q9C512
37°C, pH 6.0, substrate methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
0.00047
kifunensine
Arabidopsis thaliana
Q8H116, Q9C512
37°C, pH 6.0, substrate methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
modeling studies, molecular basis of difference in specificity, distinction of subgroup 1 and 2
additional information
-
modeling studies, molecular basis of difference in specificity, distinction of subgroup 1 and 2
additional information
-
model for substrate and conformer specificity, computational study
additional information
-
modeling studies, molecular basis of difference in specificity, distinction of subgroup 1 and 2
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
5.5 - 6
6 - 6.5
6.5
6.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 5.8
-
about half-maximal activity at pH 4 and 5.8, 0.1 M acetate buffer
5.2 - 7.3
-
about half-maximal activity at pH 5.2 and 7.3, in the presence of egg yolk lyso-phosphatidylcholine
5.5 - 7.5
-
about half-maximal activity at pH 5.5 and 7.5, in the presence of soybean phosphatidylinositol
5.5 - 7
-
about half-maximal activity at pH 5.5 and 7; (Man)8(GlcNAc)2-peptide as substrate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 60
-
45°C: optimum, 60°C: 60% of maximal activity, 65°C: 14% of maximal activity, hydrolysis of 1,2-alpha-mannobiose
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
very similar (> 60%) to other fungal 1,2-alpha-mannosidases; silveira strain, formerly known as the non-California Coccidioides immitis
Q3HYC1
UniProt
brenda
intracellular protozoan, causes Chagas’ disease in humans, epimastigote stage
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
In situ hybridization shows high levels of alpha1,2-mannosidase IB
brenda
levels of Golgi alpha1,2-mannosidase IC are similar in most tissues, with the exception of placenta and liver
brenda
-
Taka-diastase, enzyme-product from Sankyo Co.
brenda
-
commercially available under the name of Morushin
brenda
In situ hybridization shows high levels of alpha1,2-mannosidase IA; In situ hybridization shows high levels of alpha1,2-mannosidase IB
brenda
Golgi alpha1,2-mannosidase I displays distinct developmental and tissue-specific expression. Expression of Golgi alpha 1,2-mannosidases (IA, IB, IC) investigated by Nothern blot analysis and in situ hybridization; Golgi alpha1,2-mannosidase I displays distinct developmental and tissue-specific expression. Expression of Golgi alpha 1,2-mannosidases (IA, IB, IC) investigated by Nothern blot analysis and in situ hybridization. In situ hybridization shows high levels of alpha1,2-mannosidase IB; Golgi alpha1,2-mannosidase I displays distinct developmental and tissue-specific expression. Expression of Golgi alpha 1,2-mannosidases (IA, IB, IC) investigated by Nothern blot analysis and in situ hydridization
brenda
Golgi alpha1,2-mannosidase IA; Golgi alpha1,2-mannosidase IB
brenda
Golgi alpha1,2-mannosidase IA; In situ hybridization shows high levels of alpha1,2-mannosidase IB
brenda
Golgi alpha1,2-mannosidase IA; In situ hybridization shows high levels of alpha1,2-mannosidase IA; In situ hybridization shows high levels of alpha1,2-mannosidase IB, Golgi alpha1,2-mannosidase IB
brenda
Golgi alpha1,2-mannosidase IA; Golgi alpha1,2-mannosidase IB
brenda
additional information
Q3HYC1
detected in the coccidioidal T27K vaccine
brenda
-
HepG2, HepG2.2.15, AD38, and N10; HepG2, HepG2.2.15, AD38, and N10; HepG2, HepG2.2.15, AD38, and N10; HepG2, HepG2.2.15, AD38, and N10
brenda
Golgi alpha1,2-mannosidase IA; In situ hybridization shows high levels of alpha1,2-mannosidase IB; levels of Golgi alpha1,2-mannosidase IC are similar in most tissues, with the exception of placenta and liver
brenda
Golgi alpha1,2-mannosidase IA; In situ hybridization shows high levels of alpha1,2-mannosidase IA
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
with strain 22A1, the ratio of intracellular to extracellular 1,2-alpha-mannosidase activity is about 4:1
-
brenda
-
with strain 22A1, the ratio of intracellular to extracellular 1,2-alpha-mannosidase activity is about 4:1
brenda
-
2 enzymes: a membrane-bound microsomal and a soluble cytoplasmic one
brenda
-
-
brenda
-
different fusion proteins analyzed to determine if the portion of ManI located in the Golgi lumen plays a role in the targeting of this glycosidase to the Golgi and the ER membranes
brenda
different fusion proteins analyzed to determine if the portion of ManI located in the Golgi lumen plays a role in the targeting of this glycosidase to the Golgi and the ER membranes
brenda
-
different fusion proteins analyzed to determine if the portion of ManI located in the Golgi lumen plays a role in the targeting of this glycosidase to the Golgi and the ER membranes
brenda
-
different fusion proteins analyzed to determine if the portion of ManI located in the Golgi lumen plays a role in the targeting of this glycosidase to the Golgi and the ER membranes
brenda
-
2 enzymes: a membrane-bound microsomal and a soluble cytoplasmic one
brenda
-
2 enzymes: a membrane-bound microsomal and a soluble cytoplasmic one
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
blocking alpha-1,2-mannosidase in regulatory T cells results in the migration of significantly lower numbers to the peripheral lymph nodes in skin grafted mice following adoptive transfer
malfunction
-
aberrant regulation of alpha-1,2 mannosidases can result in cancer. MAN1C1 plays a role in tumor suppression in hepatocarcinogenesis. Down-regulation of MAN1C activates unfolded protein response during hepatocarcinogenesis; aberrant regulation of alpha-1,2 mannosidases can result in cancer. Upregulation of MAN1A1 activates unfolded protein response during hepatocarcinogenesis
malfunction
-
in triple KO (MAN1A1, MAN1A2, and MAN1B1) cells, Man9GlcNAc2 and Man8GlcNAc2 are the major N-glycan structures. Knockout of the MAN1A1 or MAN1A2 gene does not change the glycan profiles. Double KO cells (MAN1A1, MAN1A2) displayed increased high-mannose-type and decreased complex-type glycans. The N-glycan structures on recombinant proteins expressed in triple KO cells are simplified and changed from complex types to high-mannose types at the protein level; in triple KO (MAN1A1, MAN1A2, and MAN1B1) cells, Man9GlcNAc2 and Man8GlcNAc2 are the major N-glycan structures. Knockout of the MAN1A1 or MAN1A2 gene does not change the glycan profiles. Double KO cells (MAN1A1, MAN1A2) displayed increased high-mannose-type and decreased complex-type glycans. The N-glycan structures on recombinant proteins expressed in triple KO cells are simplified and changed from complex types to high-mannose types at the protein level; in triple KO (MAN1A1, MAN1A2, and MAN1B1) cells, Man9GlcNAc2 and Man8GlcNAc2 are the major N-glycan structures. Knockout of the MAN1A1 or MAN1A2 gene does not change the glycan profiles. Double KO cells (MAN1A1, MAN1A2) displayed increased high-mannose-type and decreased complex-type glycans. The N-glycan structures on recombinant proteins expressed in triple KO cells are simplified and changed from complex types to high-mannose types at the protein level
malfunction
abolishment of two functionally redundant mannosidases, MNS1 and MNS2, responsible for alpha-1,2-mannose trimming on the A and C branches of plant N-glycans lead to severe root growth inhibition under salt stress conditions in Arabidopsis; abolishment of two functionally redundant mannosidases, MNS1 and MNS2, responsible for alpha-1,2-mannose trimming on the A and C branches of plant N-glycans lead to severe root growth inhibition under salt stress conditions in Arabidopsis
metabolism
-
overexpression MAN1C1 shows anti-tumor effect by inducing apoptosis. MAN1C1 overexpression remarkably increases the ratio of Bax/Bcl-2 and inhibits epithelial-mesenchymal transition by increasing the expression of E-CA. In addition, the ratio of Bax/Bcl-2 and E-cadherin is increased in MAN1C1 gene overexpression renal cancer cells compared with the control cells
physiological function
-
either isozyme MANIa or MANIb can function as the Golgi alpha-mannosidase I that produces the Man5GlcNAc2 N-glycan structure necessary for complex N-glycan synthesis
physiological function
-
Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. Htm1p physically interacts with Pdi1p via its C-terminal domain
physiological function
-
alpha-1,2-mannosidase function is not required for the suppressive capacity of regulatory T cells in vitro, but influences regulatory T cell adherence in vitro andmigration in vivo
physiological function
-
key enzyme in N-glycosylation is required for the formation of mature glycoproteins in eukaryotes. MAN1A1 represents an oncogene. Upregulation of MAN1A1 activates unfolded protein response during hepatocarcinogenesis; key enzymes in N-glycosylation is required for the formation of mature glycoproteins in eukaryotes. MAN1C1 plays a role in tumor suppression in hepatocarcinogenesis. Down-regulation of MAN1C activates unfolded protein response during hepatocarcinogenesis
physiological function
the enzyme is responsible for alpha-1,2-mannose trimming on the A and C branches of plant N-glycans. MNS1/MNS2-mediated mannose trimming of N-glycans is crucial in modulating glycoprotein abundance to withstand salt stress in plants; the enzyme is responsible for alpha-1,2-mannose trimming on the A and C branches of plant N-glycans. MNS1/MNS2-mediated mannose trimming of N-glycans is crucial in modulating glycoprotein abundance to withstand salt stress in plants
physiological function
in isoforms MNS1/MNS2 double mutant, MNS3 single mutant, accumulation of Man8GlcNAc2 is observed. A triple mutant lacking mannosidases MNS1, MNS2, and MNS3, EC 3.2.1.113, reveals the almost exclusive presence of Man9GlcNAc2 glycans. The MNS triple mutants display short, radially swollen roots and altered cell walls. Pharmacological inhibition of class I alpha-mannosidases in wild-type seedlings results in a similar root phenotype; in isoforms MNS1/MNS2 double mutant, MNS3 single mutant, accumulation of Man8GlcNAc2 is observed. A triple mutant lacking mannosidases MNS1, MNS2, and MNS3, EC 3.2.1.113, reveals the almost exclusive presence of Man9GlcNAc2 glycans. The MNS triple mutants display short, radially swollen roots and altered cell walls. Pharmacological inhibition of class I alpha-mannosidases in wild-type seedlings results in a similar root phenotype
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
MNS1B_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
508
0
56289
Swiss-Prot
MNS1B_COCPS
Coccidioides posadasii (strain RMSCC 757 / Silveira)
519
1
56874
Swiss-Prot
MNS1B_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
505
0
55881
Swiss-Prot
MNS1B_NEOFI
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181)
493
0
53855
Swiss-Prot
MNS1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
521
1
60813
Swiss-Prot
MNS1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
549
1
63057
Swiss-Prot
MNS1B_ARTBC
Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)
509
0
56291
Swiss-Prot
MNS1B_ASPCL
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
511
0
56325
Swiss-Prot
MNS1B_ASPFC
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163)
493
0
53840
Swiss-Prot
MNS1B_ASPFN
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
510
0
56631
Swiss-Prot
MNS1B_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
493
0
53840
Swiss-Prot
MNS1B_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
513
0
55929
Swiss-Prot
MNS1B_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
510
0
56631
Swiss-Prot
F9D4M7_PREDD
Prevotella dentalis (strain ATCC 49559 / DSM 3688 / JCM 13448 / NCTC 12043 / ES 2772)
210
0
23926
TrEMBL
A0A0H5C042_CYBJN
Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / CCRC 20928 / JCM 3617 / NBRC 0987 / NRRL Y-1542)
166
0
18706
TrEMBL
F9D252_PREDD
Prevotella dentalis (strain ATCC 49559 / DSM 3688 / JCM 13448 / NCTC 12043 / ES 2772)
752
0
85475
TrEMBL
M5BIH6_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
239
1
27405
TrEMBL
F9D4M5_PREDD
Prevotella dentalis (strain ATCC 49559 / DSM 3688 / JCM 13448 / NCTC 12043 / ES 2772)
194
0
21839
TrEMBL
F9XHL5_ZYMTI
Zymoseptoria tritici (strain CBS 115943 / IPO323)
790
0
86918
TrEMBL
F9D4M4_PREDD
Prevotella dentalis (strain ATCC 49559 / DSM 3688 / JCM 13448 / NCTC 12043 / ES 2772)
77
0
8192
TrEMBL
A0A1R3T4A6_9BACT
744
0
85340
TrEMBL
C7PAR9_CHIPD
Chitinophaga pinensis (strain ATCC 43595 / DSM 2588 / NCIB 11800 / UQM 2034)
457
0
52805
TrEMBL
A0A0R3P124_DROPS
220
1
23731
TrEMBL
D5VI44_CAUST
Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 / TK0059)
462
0
51776
TrEMBL
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Caulobacter sp. (strain K31)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
-
analytical electrophoresis of the purified enzyme reveals two polypeptides of 52 and 23 kDa, 52000 Da polypeptide being responsible for enzyme activity as revealed by zymogram analysis
43000
-
Candida albicans CAI-4 mutant generating an active 43 kDa polypeptide. Zymogram analysis shows that the single proteolytic product of 43 kDa is able to hydrolyze the fluorogenic substrate and, this is not observed when proteolysis is blocked by pepstatin; purified alpha-mannosidase E-II remains unaltered after treatment with aspartyl protease and retains full activity on artificial substrate 4-methylumbelliferyl-alpha-D-mannopyranoside
49000
52000
56920
Q3HYC1
theoretical molecular weight. SDS-PAGE, Western blot analysis. A highly purified fraction is obtained after FPLC
63000
65000
-
detected in freshly prepared crude microsomal extracts using polyclonal antibodies, during purification the native enzyme, MW 65000, loses a membrane-spanning domain without losing its catalytic activity
79000
-
Western blotting of cell lysates, transiently expressed recombinant human ER mannosidase I is absent from mock transfected cells but detected as a single immunoreactive 79 kDa band following transient expression
460000
-
microsomal enzyme, gel filtration, presumably in a micelle or aggregate containing detergent, phospholipid or other protein
additional information
52000
-
1 * 52000, SDS-PAGE, under reducing and non-reducing conditions
52000
-
alpha1,2-mannosidase E-I. Analytical electrophoresis of the purified enzyme reveals two polypeptides of 52 and 23 kDa, 52000 Da polypeptide being responsible for enzyme activity as revealed by zymogram analysis
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
monomer
-
1 * 52000, SDS-PAGE, under reducing and non-reducing conditions
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
co-complex with an uncleaved thiodisaccharide substrate analog, hanging drop vapor diffusion method
-
crystals of both the native protein and the protein-inhibitor complex. Superimpositions are performed with LSQMAN. Comparison with human alpha-1,2-mannosidase–thiodisaccharide complex; in complex with the substrate analogue methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside, to 1.95 A resolution. The intact disaccharide spans the ?1/+1 subsites, with the D-lyxoside ring in the -1 subsite in the 1C4 chair conformation.The absence of the C5' hydroxymethyl group on the D-lyxoside moiety results in the side chain of Arg407 adopting two alternative conformations, the minor one interacting with Asp375 and the major one interacting with both the D-lyxoside and the catalytic base Glu409, thus disrupting its function
native protein and in complex with inhibitor kifunensine or 1-deoxymannojirimycin
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
C443G
-
Tm-value of mutant enzyme is 50.2°C compared to 55.8°C for the wild-type enzyme
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
D463N
D463N/E599Q
-
pH-optimum is 6.6 compared to 7.1 for wild-type enzyme, kcat/Km is 8.3fold lower than wild-type value
E330Q
E330Q/E599Q
-
pH-optimum is 6.6 compared to 7.1 for wild-type enzyme, kcat/Km is 340000fold lower than wild-type value
E599Q
F659A
H524A
-
pH-optimum is 6.9 compared to 7.1 for wild-type enzyme, kcat/Km is 28.3fold lower than wild-type value
R334A
-
mutant enzyme is not detected in the culture medium, kcat/Km is 28.3fold lower than wild-type v