Information on EC 2.4.1.131 - GDP-Man:Man3GlcNAc2-PP-dolichol alpha-1,2-mannosyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
2.4.1.131
-
RECOMMENDED NAME
GeneOntology No.
GDP-Man:Man3GlcNAc2-PP-dolichol alpha-1,2-mannosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = 2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
dolichyl-diphosphooligosaccharide biosynthesis
-
Metabolic pathways
-
N-Glycan biosynthesis
-
Various types of N-glycan biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
GDP-alpha-D-mannose:D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol 2-alpha-D-mannosyltransferase
The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in alpha(1->2) linkages to the nascent oligosaccharide.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Alg11
P53954
gene name
Alg11
O74878
gene name
Alg2 mannosyltransferase
-
-
At2G40190
-
gene name
galactomannan deficiency protein 3
O74878
-
GDP-Man:Man3GlcNAc2-PP-dolichol-alpha1,2-mannosyltransferase
Q2TAA5
-
GDP-mannose-oligosaccharide-lipid mannosyltransferase
-
-
-
-
gmd3
O74878
gene name
guanosine diphosphomannose-oligosaccharide-lipid mannosyltransferase
-
-
-
-
hALG11
Q2TAA5
-
LEW3
-
gene name
mannosyltransferase, guanosine diphosphomannose-oligosaccharide-lipid
-
-
-
-
oligosaccharide-lipid mannosyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
74506-43-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
cow
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
; New Zealand white rabbits
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
compared with wild-type cells, DELTAalg11 grows poorly and osmotic stabilization by KCl only slightly improved growth. Deletion of ALG11 causes a temperature-sensitive lethality between 32C and 36C
malfunction
-, Q2TAA5
a patient with muscular hypotonia, convulsions, developmental retardation, dysmorphic signs and death in infancy, a deficiency of GDP-Man:Man3GlcNAc2-PP-dolichol mannosyltransferase, the human ortholog of Alg11 from yeast, is identified as the molecular cause. The enzymatic malfunction leads to impairment in the elongation of lipid-linked oligosaccharides at the outer leaflet of the endoplasmic reticulum, resulting in CDG-Ip, a congenital disorders of glycosylation. Mutation p.L86S in the endoplasmic reticulum mannosyltransferase hALG11 leads to accumulation of Man3GlcNAc2-PP-dolichol and Man4GlcNAc2-PP-dolichol in the index CDG-Ip patient
malfunction
-
a deletion of the ALG11 gene leads to poor growth and temperature-sensitive lethality, disruption of the ALG11 locus results in Underglycosylation of proteins
malfunction
-
mutant lew3, which has a defect in alpha-1,2-mannosyltransferase is deficient in N-glycosylation
malfunction
O74878
gmd3 mutant cannot grow at 37C. Construction of a plasmid pREP1+/-ALG11HA for the expression of Saccharomyces cerevisiae ALG11 in Schizosaccharomyces pombe and introducing it into gmd3 mutant. The gmd3 mutant, carrying pREP+/-ALG11HA, grows at 37C, whereas the gmd3 mutant, carrying vector pREP1 alone, does not. The defect in acid phosphatase glycosylation of gmd3 mutant is also suppressed by Saccharomyces cerevisiae ALG11. The gmd3+/alg11+ gene is a functional homologue of the Saccharomyces cerevisiae ALG11 gene
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 GDP-D-mannose + D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
show the reaction diagram
-
-
-
-
?
2 GDP-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
show the reaction diagram
P53954, -
-
-
-
?
2 GDP-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
show the reaction diagram
-
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol. Biosynthesis of asparagine-linked glycoproteins, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway
-
-
?
2 GDP-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
show the reaction diagram
P53954, -
the biosynthesis of asparagine-linked glycans occurs in an evolutionarily conserved manner with the assembly of the unique lipid-linked oligosaccharide precursor Glc3Man9GlcNAc2-PPDo at the endoplasmic reticulum. The enzyme catalyzes the transfer of two alpha1,2-linked mannose residues from GDP-mannose to Man3GlcNAc2-PP-Dol and subsequently to Man4GlcNAc2-PP-Dol forming the Man5GlcNAc2-PP-Dol intermediate at the cytosolic side of the endoplasmic reticulum before flipping to the luminal side
-
-
?
2 GDP-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
show the reaction diagram
-
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol
-
-
?
GDP-mannose + lipid-linked Manalpha(1-3)Manbeta-GlcNAcbeta-GlcNAc
GDP + lipid-linked Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-6))Manbeta-GlcNAcbeta-GlcNAc
show the reaction diagram
-
reaction via penta- and hexasaccharide intermediates to a lipid-linked heptasaccharide, presumably multiple mannosyltransferases involved
-
?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
show the reaction diagram
-
oligosaccharide portion: a mixture of trisaccharide and pentasaccharide, acceptor lipids are probably Manbeta-GlcNAc-GlcNAc-pyrophosphoryldolichol and Man2alpha-Manbeta-GlcNAc-GlcNAc-pyrophosphoryldolichol
heptasaccharide-lipid as product, probably Man5GlcNAc2 as heptasaacharide
?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
show the reaction diagram
-
oligosaccharide-P-P-lipid: major oligosaccharide component is Man2GlcNAc2
penta-, hexa-, and heptasaccharide as oligosaccharide portion, formed by the stepwise addition of mannose to the growing oligosaccharide chain
?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
show the reaction diagram
-
acceptor isolated from pig liver
heptasaccharide-lipid as product, probably Man5GlcNAc2 as heptasaacharide
?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
show the reaction diagram
-
acceptor isolated from pig liver
presumably a heptasaccharide with a 1,6-linked branched glycosyl unit with 65% of the newly added mannosyl units in a terminal nonreducing position, structure may be Manalpha(1-2)Man-Man(Man(1-6))Man-GlcNAc-GlcNAc
?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
show the reaction diagram
-
acceptor isolated from pig liver
penta-, hexa-, and heptasaccharide as oligosaccharide portion, formed by the stepwise addition of mannose to the growing oligosaccharide chain
?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
show the reaction diagram
-
acceptors can be mannose or Man-(GlcNAc)2 to (Man)5-(GlcNAc)2, lipid-linked tetrasaccharide Manalpha(1-3)Manbeta-GlcNAcbeta-GlcNAc, presumably multiple mannosyltransferases involved, acceptor isolated from baby hamster kidney cells, i.e. BHK cells
-
?
GDPmannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
show the reaction diagram
-
involved in biosynthesis of lipid-linked oligosaccharides up to (Man)5-(GlcNAc)2, involved in the production of two 1,2-linked mannosyl residues in mammalian lipid-linked tetradecasaccharide of the structure (Glc)3(Man)9(GlcNAc)2, the major precursor for eukaryotic en-bloc-glycosylation of asparagin-linked glycoproteins
-
-
-
GDPmannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
show the reaction diagram
-
biosynthesis of oligosaccharide-lipids
-
-
-
additional information
?
-
-
involved in asparagine-linked glycosylation, reaction proceeds in the endoplasmatic reticulum, role of the ALG9 step in downstream ER and Golgi N-glycan processing events
-
-
-
additional information
?
-
-
Alg11 mannosyltransferase shows no activity with Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol
-
-
-
additional information
additional information
-
-
no substrate: dolichol-phosphat
-
-
-
additional information
additional information
-
-
no substrate: dolichol-phosphat
-
-
-
additional information
additional information
-
-
no sugar donor: mannosylphosphoryldolichol
-
-
-
additional information
additional information
-
-
no sugar donor: mannosylphosphorylretinol
-
-
-
additional information
additional information
-
-
(Man)6-(GlcNAc)2 precursor of enzyme
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-2)Manalpha(1-3)Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAcalpha/beta is the product of the middle-arm terminal alpha1,2-mannosyltransferase Alg9p
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 GDP-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
show the reaction diagram
-
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol. Biosynthesis of asparagine-linked glycoproteins, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway
-
-
?
2 GDP-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
show the reaction diagram
P53954, -
the biosynthesis of asparagine-linked glycans occurs in an evolutionarily conserved manner with the assembly of the unique lipid-linked oligosaccharide precursor Glc3Man9GlcNAc2-PPDo at the endoplasmic reticulum. The enzyme catalyzes the transfer of two alpha1,2-linked mannose residues from GDP-mannose to Man3GlcNAc2-PP-Dol and subsequently to Man4GlcNAc2-PP-Dol forming the Man5GlcNAc2-PP-Dol intermediate at the cytosolic side of the endoplasmic reticulum before flipping to the luminal side
-
-
?
GDPmannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
show the reaction diagram
-
involved in biosynthesis of lipid-linked oligosaccharides up to (Man)5-(GlcNAc)2, involved in the production of two 1,2-linked mannosyl residues in mammalian lipid-linked tetradecasaccharide of the structure (Glc)3(Man)9(GlcNAc)2, the major precursor for eukaryotic en-bloc-glycosylation of asparagin-linked glycoproteins
-
-
-
GDPmannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
show the reaction diagram
-
biosynthesis of oligosaccharide-lipids
-
-
-
additional information
?
-
-
involved in asparagine-linked glycosylation, reaction proceeds in the endoplasmatic reticulum, role of the ALG9 step in downstream ER and Golgi N-glycan processing events
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
no requirement of divalent cations; reaction is independent of the addition of divalent cations
additional information
-
no requirement of divalent cations
additional information
-
no requirement of divalent cations
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
-
2 mM, less than 15% inhibition
ATP
-
2 mM, less than 15% inhibition
Ca2+
-
weak
Cu2+
-
strong
GDP
-
0.02 mM, 84% inhibition; 2 mM, 84% inhibition
GMP
-
0.02 mM, 30% inhibition; 2 mM, 30% inhibition
GTP
-
0.02 mM, 40% inhibition; 2 mM, 40% inhibition
UDP
-
2 mM, less than 15% inhibition
UDP-galactose
-
2 mM, less than 15% inhibition
UDP-glucose
-
2 mM, less than 15% inhibition
UDP-N-acetylglucosamine
-
2 mM, less than 15% inhibition
additional information
-
less than 15% inhibition at 2 mM: ADP, ATP, UDP, UDP-glucose, UDP-galactose and UDP-N-acetylglucosamine; not inhibited by EDTA
-
additional information
-
not inhibited by amphomycin; not inhibited by EDTA
-
additional information
-
not inhibited by amphomycin; not inhibited by EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-
slight stimulation
Endogen lipids
-
soluble in CHCl3/CH3OH, 2:1, activation
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00064
-
D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
pH 7.0, 37C
0.0047
-
GDP-D-mannose
-
pH 7.0, 37C
0.0047
-
GDPmannose
-
-
0.00064
-
oligosaccharide-lipid acceptor
-
based on the assumption of incorporation of only a single mannosyl unit into the product
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
7.6
-
broad
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
intimal layer
Manually annotated by BRENDA team
-
expressed especially in developing stems and flowers
Manually annotated by BRENDA team
-
lactating mammary tissue
Manually annotated by BRENDA team
-
expressed especially in developing stems and flowers
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases
Manually annotated by BRENDA team
-
membrane-bound
Manually annotated by BRENDA team
-
membrane-bound
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
63140
-
-
calculated from sequence
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 63143, calculated from sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no glycoprotein
-
the protein is predicted to contain four N-linked glycosylation sites, but none appear to be utilized, because Alg11p is insensitive to digestion with endo H
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, solubilized enzyme, 2 weeks: about 40% loss of activity, 7 days: about 20% loss of activity
-
0-4C, solubilized enzyme, at least 2 weeks, stable
-
0C, partially purified enzyme, 5 days, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partial; solubilized with 0.15% v/v Nonidet P-40, partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
transformation of the LEW3 gene into the yeast mutant alg11, which exhibits a lowtemperature-sensitive phenotype and grows slowly at and below 30C but normally at 37C. Expression of LEW3 partially complements the slow-growth phenotype of the yeast mutant alg11, suggesting that the plant ALG11 homolog is able to partially substitute for the function of ALG11 in yeast
-
retroviral expression of human wild-type and mutated ALG11 cDNA in patient-derived fibroblasts as well as using a yeast alg11 deletion strain as a heterologous expression system for hALG11 variants
-, Q2TAA5
ALG9 gene encodes a middle-arm terminal alpha1,2-mannosyltransferase Alg9p
-
construction of a plasmid pREP1+/-ALG11HA for the expression of Saccharomyces cerevisiae ALG11 in Schizosaccharomyces pombe and introducing it into gmd3 mutant. The gmd3 mutant, carrying pREP+/-ALG11HA, grows at 37C, whereas the gmd3 mutant, carrying vector pREP1 alone, does not. The defect in acid phosphatase glycosylation of gmd3 mutant is also suppressed by Saccharomyces cerevisiae ALG11. The gmd3+/alg11+ gene is a functional homologue of the Saccharomyces cerevisiae ALG11 gene
-
overexpression in Escherichia coli. Two Alg2 constructs are expressed and isolated, one with the N-terminal TRX domain and C-terminal His and V5 epitope tags and the other with only an N-terminal His tag
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
L85A
-, Q2TAA5
no effect on Alg11 mannosyltransferase activity
L86P
-, Q2TAA5
mutant enzyme does not complement the growth deffect of the mutant strain DELTAalgg3 (Saccharomyces cerevisiae)
L86S
-, Q2TAA5
mutant enzyme slightly complements the growth deffect of the mutant strain DELTAalgg3 (Saccharomyces cerevisiae)
E318A
-
mutation has no effect on activity
E356A
-
mutation has no effect on activity
E405/H406A
-
double mutant no longer supports growth, the loss of activity is not caused by a failure of Alg11 expression
E405A
-
mutation causes an underglycosylation of the vacuolar model glycoproteincarboxypeptidase Y
E405A
-
mutation causes nearly complete abrogation of product formation
E405A/E413
-
double mutant no longer supports growth, the loss of activity is not caused by a failure of Alg11 expression
E405A/E413A
-
completely inactive mutant enzyme
E413A
-
mutation has no effect
E413A
-
activity is indistinguishable from that of the wild-type under comparable conditions
F407A
-
mutation is not detrimental for growth, impairment of glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
G84A
-
mutation has no effect on growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
G84P
-
mutation reduces growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
G85A
-
mutation has no effect on growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
G85P
-
mutation reduces growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
G87A
-
mutation has no effect on growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
G87P
-
mutation reduces growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
H406A
-
mutation is not detrimental for growth, impairment of glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
K302A
-
mutation has no effect on activity
K319A
-
mutation causes loss of Alg11 activity
K322A
-
mutation has no effect on activity
K343A
-
mutation has no effect on activity
V412A
-
mutation is not detrimental for growth