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Information on EC 3.2.1.209 - endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase and Organism(s) Candida albicans and UniProt Accession Q8J0Q0
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3.2.1.209 endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidaseIUBMB Comments
The enzyme, located in the endoplasmic reticulum, primarily trims a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2 isomer 8A1,2,3B1,3 (the names of the isomers listed here are based on a nomenclature system proposed by Prien et al ). The removal of the single mannosyl residue occurs in all eukaryotes as part of the processing of N-glycosylated proteins, and is absolutely essential for further elongation of the outer chain of properly-folded N-glycosylated proteins in yeast. In addition, the enzyme is involved in glycoprotein quality control at the ER quality control compartment (ERQC), helping to target misfolded glycoproteins for degradation. When present at very high concentrations in the ERQC, the enzyme can trim the carbohydrate chain further to Man(5-6)GlcNAc2.
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Word Map
- 3.2.1.209
-
er-associated
-
misfolded
-
trim
- n-glycans
- calnexin
-
edems
-
reticulum-associated
- kifunensine
- man8glcnac2
-
degradation-enhancing
-
retrotranslocation
-
er-derived
-
mannose-trimming
- 1-deoxymannojirimycin
-
p58ipk
-
xtp3-b
The taxonomic range for the selected organisms is: Candida albicans
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
edem1, ermani, edem3, er mannosidase i, alpha1,2-mannosidases, alpha1,2-mannosidase e-i, er mani, class i alpha1,2-mannosidase, er alpha1,2-mannosidase i, endoplasmic reticulum alpha1,2-mannosidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MAN1B1
-
-
-
-
MNS1
-
-
-
-
MNS3
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Man9GlcNAc2-[protein]2-alpha-mannohydrolase (configuration-inverting)
The enzyme, located in the endoplasmic reticulum, primarily trims a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2 isomer 8A1,2,3B1,3 (the names of the isomers listed here are based on a nomenclature system proposed by Prien et al [7]). The removal of the single mannosyl residue occurs in all eukaryotes as part of the processing of N-glycosylated proteins, and is absolutely essential for further elongation of the outer chain of properly-folded N-glycosylated proteins in yeast. In addition, the enzyme is involved in glycoprotein quality control at the ER quality control compartment (ERQC), helping to target misfolded glycoproteins for degradation. When present at very high concentrations in the ERQC, the enzyme can trim the carbohydrate chain further to Man(5-6)GlcNAc2.
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
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannose
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + D-mannopyranose
-
-
-
?
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)GlcNAc + H2O
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 + 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(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
cytosolic isoform E-I
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside
4-methylumbelliferone + D-mannose
-
MUaMan, fluorogenic substrate
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + D-mannose
-
MUaMan fluorogenic substrate to measure enzyme activity
-
-
?
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
? + D-mannose
-
to measure enzyme activity
-
-
?
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 + H2O
? + D-mannose
-
to measure enzyme activity
-
-
?
additional information
?
-
enzyme is involved in the processing of N-linked mannans
-
-
?
additional information
?
-
-
enzyme is involved in the processing of N-linked mannans
-
-
?
additional information
?
-
cytosolic isoform E-I trims free Man8GlcNac2 isomer B into Man7GlcNac2 isomer B
-
-
?
additional information
?
-
-
cytosolic isoform E-I trims free Man8GlcNac2 isomer B into Man7GlcNac2 isomer B
-
-
?
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(1-2)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(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
cytosolic isoform E-I
-
-
?
additional information
?
-
enzyme is involved in the processing of N-linked mannans
-
-
?
additional information
?
-
-
enzyme is involved in the processing of N-linked mannans
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pepstatin A
-
in the presence of mixed membrane fraction from strain ATTC 26555, the 52 kDa polypeptide is converted into a 43 kDa active product. Protease inhibitors, such as phenylmethylsulphonylfluoride, trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane and 1,10-phenantroline, fail to prevent proteolysis. Pepstatin A, an aspartyl protease inhibitor, fully blocked enzyme processing
1-deoxymannojirimycin
-
DMJ, inhibition of 4-methylumbelliferyl-alpha-D-mannopyranoside hydrolysis
1-deoxymannojirimycin
-
trimming is inhibited preferentially by 1-deoxymannojirimycin, inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
swainsonine
-
inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
swainsonine
-
SW, inhibition of 4-methylumbelliferyl-alpha-D-mannopyranoside hydrolysis
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
4-methylumbelliferyl-alpha-D-mannopyranoside
-
hydrolysis of the fluorogenic substrate follows hyperbolic kinetics
0.11
4-methylumbelliferyl-alpha-D-mannopyranoside
-
MUaMan, fluorogenic substrate. Vmax 36.2 nmol of 4-methylumbelliferone min-1 mg-1 of protein
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
1-deoxymannojirimycin
Candida albicans
-
inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
0.23
1-deoxymannojirimycin
Candida albicans
-
inhibition of 4-methylumbelliferyl-alpha-D-mannopyranoside hydrolysis
0.47
swainsonine
Candida albicans
-
inhibition of 4-methylumbelliferyl-alpha-D-mannopyranoside hydrolysis
0.55
swainsonine
Candida albicans
-
inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00003
-
purification of soluble alpha-mannosidase from CAI-4 strain, High-speed supernatant used to measure alpha-mannosidase activity
0.00008
-
purification of soluble alpha-mannosidase from CAI-4 strain, Sepharose CL6B
0.0002
-
mixed membrane fraction (MMF) of ATCC 26555 supernatant, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0005
0.0012
-
mixed membrane fraction (MMF) of CAI-4 and ATCC 26555 pellet, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0019
-
mixed membrane fraction (MMF) of ATCC 26555 pellet, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0021
-
purification of soluble alpha-mannosidase from CAI-4 strain, DEAE Bio-Gel A
0.0022
-
mixed membrane fraction (MMF) of CAI-4 and ATCC 26555 plus 1 mM pepstatin pellet, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0026
-
mixed membrane fraction (MMF) of CAI-4 pellet, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.003
-
purification of soluble alpha-mannosidase from CAI-4 strain, Sephadex G-25
0.0047
-
mixed membrane fraction (MMF) of CAI-4 and ATCC 26555 supernatant, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0057
-
purification of soluble alpha-mannosidase from CAI-4 strain, DEAE Bio-Gel A
0.0101
-
purification of soluble alpha-mannosidase from CAI-4 strain, Con A-Sepharose
0.0108
-
purification of soluble alpha-mannosidase from CAI-4 strain, Sephadex G-25
additional information
-
hydrolysis of the fluorogenic substrate 4-methylumbelliferyl-alpha-D-mannopyranoside follows hyperbolic kinetics and LineweaverBurk plots reveals Vmax values of 30.9 nmol of methylumbelliferone min-1 mg-1 of protein
0.0005
-
mixed membrane fraction (MMF) of CAI-4 and ATCC 26555 plus 1 mM pepstatin supernatant, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0005
-
mixed membrane fraction (MMF) of CAI-4 supernatant, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
presence of a 65000 Da membrane-bound isoform that is cleaved by protease Kex2 to soluble 52000 Da isoform E-I
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
65000
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
27000
-
analytical electrophoresis of the purified preparation reveals two polypeptides
43000
52000
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
43000
-
converting the 52 kDa alpha-mannosidase into a polypeptide of 43 kDa retaining full enzyme activity demonstrated in membranes of ATCC 26555, support a precursor-product relationship between soluble alpha1,2-mannosidase E-I (52 kDa) and alpha1,2-mannosidase E-II (43 kDa)
43000
-
purified alpha-mannosidase E-II remains unaltered after treatment with aspartyl protease and retains full activity on artificial substrate 4-methylumbelliferyl-alpha-D-mannopyranoside
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
52000
-
analytical electrophoresis of the purified preparation reveals two polypeptides. Responsible for enzyme activity. Active on the fluorogenic substrate 4-methylumbelliferyl-alpha-D-mannopyranoside as revealed by zymogram analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by conventional methods of protein isolation and affinity chromatography in Concanavalin A-Sepharose 4B. Alpha-mannosidase E-I is purified by a fungal aspartyl protease
-
ion exchange chromatography, used to measure protein and enzyme activity, Sepharose CL6B, DEAE Bio-Gel A, Sephadex G-25, DEAE Bio-Gel A, Con A-Sepharose, Sephadex G-25
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mora-Montes, H.M.; Lopez-Romero, E.; Zinker, S.; Ponce-Noyola, P.; Flores-Carreon, A.
Conversion of alpha1,2-mannosidase E-I from Candida albicans to alpha1,2-mannosidase E-II by limited proteolysis
Antonie van Leeuwenhoek
93
61-69
2008
Candida albicans
Mora-Montes, H.M.; Lopez-Romero, E.; Zinker, S.; Ponce-Noyola, P.; Flores-Carreon, A.
Purification of soluble alpha1,2-mannosidase from Candida albicans CAI-4
FEMS Microbiol. Lett.
256
50-56
2006
Candida albicans
Mora-Montes, H.M.; Lopez-Romero, E.; Zinker, S.; Ponce-Noyola, P.; Flores-Carreon, A.
Heterologous expression and biochemical characterization of an alpha1,2-mannosidase encoded by the Candida albicans MNS1 gene
Mem. Inst. Oswaldo Cruz
103
724-730
2008
Candida albicans (Q8J0Q0), Candida albicans
Mora-Montes, H.M.; Bader, O.; Lopez-Romero, E.; Zinker, S.; Ponce-Noyola, P.; Hube, B.; Gow, N.A.; Flores-Carreon, A.
Kex2 protease converts the endoplasmic reticulum alpha1,2-mannosidase of Candida albicans into a soluble cytosolic form
Microbiology
154
3782-3794
2008
Candida albicans (Q8J0Q0), Candida albicans, Candida albicans ATCC 26555 (Q8J0Q0)
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