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Information on EC 2.4.1.232 - initiation-specific alpha-1,6-mannosyltransferase
for references in articles please use BRENDA:EC2.4.1.232
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.232 initiation-specific alpha-1,6-mannosyltransferase
IUBMB Comments
Requires Mn2+. In Saccharomyces cerevisiae, this enzyme catalyses an essential step in the outer chain elongation of N-linked oligosaccharides. Man8GlcNAc and Man9GlcNAc are equally good substrates.
The enzyme appears in viruses and cellular organisms
- 2.4.1.232
- mannans
-
mannoproteins
-
alpha-1,6-linked
- alpha-1,2-mannosidase
- man8glcnac2
-
pyridylaminated
- mannoses
-
cis-golgi
-
man5glcnac2-pp-dol
-
polymannose
- drug development
showSynonyms
och1p, mnn9p, alpha-1,6-mannosyltransferase, alpha-mannosyltransferase, spoch1p, anp1p, hpoch1, yloch1p, tbalg12, vdoch1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AFUA_2G01450
alpha-1,6-mannosyltransferase
alpha-1,6-MT
alpha-mannosyltransferase
Anl1p
GDP-mannose:glycolipid 1,6-alpha-D-mannosyltransferase
GDP-mannose:oligosaccharide 1,6-alpha-D-mannosyltransferase
-
-
-
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glycolipid 6-alpha-mannosyltransferase
mannosyltransferase, guanosine diphosphomannose-glycoprotein alpha1-6-
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Mnn9
Mnn9p
Och1p
ScMnn9p
alpha-1,6-mannosyltransferase
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-
-
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GDP-mannose:glycolipid 1,6-alpha-D-mannosyltransferase
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-
-
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glycolipid 6-alpha-mannosyltransferase
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-
-
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Mnn9p
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Saccharomyces cerevisiae, part of two elongating alpha-1,6-mannosyltransferase complexes
Och1p
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Saccharomyces cerevisiae, initiating alpha-1,6-mannosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-mannose linkage
Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-mannose linkage
requires Mn2+. In Saccharomyces cerevisiae, this enzyme catalyses an essential step in the outer chain elongation of N-linked oligosaccharides. Man8GlcNAc and Man9GlcNAc are equally good substrates
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-
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Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-mannose linkage
requires Mn2+, in Saccharomyces cerevisiae, this enzyme catalyses an essential step in the outer chain elongation of N-linked oligosaccharides, Man8GlcNAc and Man9GlcNAc are equally good substrates
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
hexosyl group transfer
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-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
protein N-glycosylation processing of mannoproteins (cis-Golgi, yeast), protein N-glycosylation processing of proteins targeted for retention in cellular organelles (cis-Golgi, yeast)
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SYSTEMATIC NAME
IUBMB Comments
GDP-mannose:oligosaccharide 6-alpha-D-mannosyltransferase
Requires Mn2+. In Saccharomyces cerevisiae, this enzyme catalyses an essential step in the outer chain elongation of N-linked oligosaccharides. Man8GlcNAc and Man9GlcNAc are equally good substrates.
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CAS REGISTRY NUMBER
COMMENTARY
135622-87-6
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346003-17-6
Schizosaccharomyces pombe gene och1+
346003-17-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-alpha-D-Man + GDP-mannose
4-methylumbelliferyl-alpha-D-Man-(1->6)-D-Man + GDP
alpha-D-mannose + 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-pyridylamine
?
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Substrates: recombinant enzyme shows 28.8% of the activity with 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-pyridylamine
Products: -
Products: -
?
GDP-mannose + (GlcNAc)2(Man)9(Asn)1
GDP + (GlcNac)2(Man)10(Asn)1
Substrates: -
Products: -
Products: -
?
GDP-mannose + alpha-1,6-D-mannobiose
?
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Substrates: two distinct Mnn9p-containing multi-protein complexes add multiple mannosyl residues forming a series of poly-mannose structures in vitro, no substrate of Och1p
Products: formation of a series of poly-mannose structures, which contain mainly alpha-1,6- and some additional alpha-1,2-linked mannoses
Products: formation of a series of poly-mannose structures, which contain mainly alpha-1,6- and some additional alpha-1,2-linked mannoses
?
GDP-mannose + Man8GlcNAc
GDP + Man9GlcNAc
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Substrates: Man8GlcNAc from thyroglobulin Man9GlcNAc by treatment with yeast specific mannosidase, specificity, enzyme catalyzes addition of mannose to the alpha-1,3-mannose of the substrate, initiates outer chain formation
Products: -
Products: -
?
GDP-mannose + Man9GlcNAc
GDP + Man10GlcNAc
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Substrates: Man9GlcNAc from thyroglobulin, specificity, enzyme catalyzes addition of mannose to the alpha-1,3-mannose of the substrate, initiates outer chain formation
Products: -
Products: -
?
GDP-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-pyridylamine
?
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Substrates: recombinant enzyme shows 74.2% of the activity with 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-pyridylamine. Och1p has the catalytic potential to transfer two molecules of mannose to 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-pyridylamine. The second mannose is attached with alpha1,6-linkage to either the alpha1,6-linked or the alpha1,3-linked mannose that is attached to alpha1,6-linked mannose
Products: -
Products: -
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GDP-mannose + Manalpha(1,2)Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-pyridylamine
?
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Substrates: recombinant enzyme shows 58.5% of the activity with 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-pyridylamine
Products: -
Products: -
?
GDP-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-pyridylamine
?
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Substrates: -
Products: -
Products: -
?
GDP-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-pyridylamine
?
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Substrates: recombinant enzyme shows 66.1% of the activity with 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-pyridylamine
Products: -
Products: -
?
GDP-mannose + 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-pyridylamine
?
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Substrates: recombinant enzyme shows 28.8% of the activity with 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-pyridylamine
Products: -
Products: -
?
GDP-mannose + Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-pyridylamine
?
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Substrates: recombinant enzyme shows 14.4% of the activity with 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-pyridylamine
Products: -
Products: -
?
GDP-mannose + Manalpha(1,6)[Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-pyridylamine
?
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Substrates: recombinant enzyme shows 14.4% of the activity with 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-pyridylamine
Products: -
Products: -
?
GDP-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
GDP + Manalpha(1-2)[Manalpha(1-6)]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
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Substrates: Man9GlcNAc from rat liver glycoproteins and thyroglobulin, enzyme initiates outer chain synthesis, the mannose residue added is alpha-1,6-linked to the alpha-1,6-mannose residue of the substrate, removal of the alpha-1,2-linked mannose residue from Man9GlcNAc is not essential for enzyme activity
Products: Man10GlcNAc
Products: Man10GlcNAc
?
GDP-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
GDP + Manalpha(1-2)[Manalpha(1-6)]Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAc
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Substrates: Man8GlcNAc from rat liver glycoproteins and thyroglobulin, enzyme initiates outer chain synthesis, the mannose residue added is alpha-1,6-linked to the alpha-1,6-mannose residue of the substrate
Products: Man9GlcNAc
Products: Man9GlcNAc
?
GDP-mannose + Manalpha(1-3)Manalpha(1-2)Manalpha(1-3)Manalpha(1-2)Man
GDP + Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-2)Manalpha(1-2)Manalpha(1-2)Man
GDP-mannose + oligosaccharide acceptor
?
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Substrates: Mnn9p is involved in protein mannosylation, incorporates alpha-1,6-linked mannose residues, the elongation of the N-glycan outer chain, initiated by Och1p, is continued by two mannosyltransferase complexes: V-complex composed of Mnn9p and Van1p and A-complex composed of Mnn9p, Anp1p, Hoc1p, Mnn10p and Mnn11p
Products: -
Products: -
?
GDP-mannose + pyridylaminated Man5GlcNAc2
GDP + pyridylaminated Man6GlcNAc2
Substrates: incorporates alpha-1,6-linked mannose, poor substrate
Products: -
Products: -
?
GDP-mannose + pyridylaminated Man6GlcNAc2
GDP + pyridylaminated Man7GlcNAc2
Substrates: incorporates alpha-1,6-linked mannose
Products: -
Products: -
?
GDP-mannose + pyridylaminated Man7GlcNAc2
GDP + pyridylaminated Man8GlcNAc2
Substrates: incorporates alpha-1,6-linked mannose
Products: -
Products: -
?
GDP-mannose + pyridylaminated Man8GlcNAc2
GDP + pyridylaminated Man9GlcNAc2
Substrates: incorporates alpha-1,6-linked mannose
Products: -
Products: -
?
GDP-mannose + pyridylaminated Man9GlcNAc2
GDP + pyridylaminated Man10GlcNAc2
Substrates: incorporates alpha-1,6-linked mannose
Products: -
Products: -
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
GDP + pyridylaminated alpha-mannosyl-1,6-oligosaccharide
Substrates: incorporates alpha-1,6-linked mannose, substrate specificity
Products: -
Products: -
?
4-methylumbelliferyl-alpha-D-Man + GDP-mannose
4-methylumbelliferyl-alpha-D-Man-(1->6)-D-Man + GDP
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-D-Man + GDP-mannose
4-methylumbelliferyl-alpha-D-Man-(1->6)-D-Man + GDP
Substrates: -
Products: -
Products: -
?
GDP-mannose + 6-O-alpha-D-mannopyranosyl-D-mannopyranose
GDP + alpha-(1->6)-D-mannotriose
Substrates: -
Products: -
Products: -
?
GDP-mannose + 6-O-alpha-D-mannopyranosyl-D-mannopyranose
GDP + alpha-(1->6)-D-mannotriose
Substrates: -
Products: -
Products: -
?
GDP-mannose + Man8GlcNAc2-PA
GDP + Man9GlcNAc2-PA
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Substrates: best acceptor for Och1p, initiation-specific alpha-1,6-mannosyltransferase that requires the intact structure of Man8GlcNAc for efficient mannose outer chain initiation
Products: additional Man is attached with an alpha-1,6-linkage at the site where mannose outer chain elongation initiates
Products: additional Man is attached with an alpha-1,6-linkage at the site where mannose outer chain elongation initiates
?
GDP-mannose + Man8GlcNAc2-PA
GDP + Man9GlcNAc2-PA
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Substrates: best acceptor for Och1p, initiation-specific alpha-1,6-mannosyltransferase that requires the intact structure of Man8GlcNAc for efficient mannose outer chain initiation
Products: additional Man is attached with an alpha-1,6-linkage at the site where mannose outer chain elongation initiates
Products: additional Man is attached with an alpha-1,6-linkage at the site where mannose outer chain elongation initiates
?
GDP-mannose + Man9GlcNAc2-PA
GDP + Man10GlcNAc2-PA
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Substrates: enzyme incorporates alpha-1,6-linked mannose into the substrate
Products: -
Products: -
?
GDP-mannose + Man9GlcNAc2-PA
GDP + Man10GlcNAc2-PA
-
Substrates: enzyme incorporates alpha-1,6-linked mannose into the substrate
Products: -
Products: -
?
GDP-mannose + Manalpha(1-3)Manalpha(1-2)Manalpha(1-3)Manalpha(1-2)Man
GDP + Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-2)Manalpha(1-2)Manalpha(1-2)Man
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Substrates: mannopentaose from Candida albicans, substrate specificity study, structural requirement of enzyme is Manalpha(1-3)Manalpha(1-)
Products: structure, presence of an alpha-1,6 branching mannose unit
Products: structure, presence of an alpha-1,6 branching mannose unit
?
GDP-mannose + Manalpha(1-3)Manalpha(1-2)Manalpha(1-3)Manalpha(1-2)Man
GDP + Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-2)Manalpha(1-2)Manalpha(1-2)Man
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Substrates: mannopentaose from Candida albicans, substrate specificity study, structural requirement of enzyme is Manalpha(1-3)Manalpha(1-)
Products: structure, presence of an alpha-1,6 branching mannose unit
Products: structure, presence of an alpha-1,6 branching mannose unit
?
GDP-mannose + oligosaccharide acceptor
GDP + alpha-mannosyl-1,6-oligosaccharide
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Substrates: Mnn9p incorporates alpha-1,6-linked mannose residues, the elongation of the N-glycan outer chain, initiated by Och1p, is continued by two mannosyltransferase complexes: V-complex composed of Mnn9p and Van1p and A-complex composed of Mnn9p, Anp1p, Hoc1p, Mnn10p and Mnn11p, study of the interactions between the subunits of the mannosyltransferase complexes
Products: -
Products: -
?
GDP-mannose + oligosaccharide acceptor
GDP + alpha-mannosyl-1,6-oligosaccharide
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Substrates: Mnn9p is a component of two distinct multi-protein complexes, both having alpha-1,6-mannosyltransferase activity: a complex of Mnn9p and Van1p and a complex of Mnn9p, Anp1p, Mnn10p, Mnn11p and Hoc1p
Products: -
Products: -
?
GDP-mannose + oligosaccharide acceptor
GDP + alpha-mannosyl-1,6-oligosaccharide
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Substrates: Mnn9p is associated in two distinct multi-protein complexes, both having alpha-1,6-mannosyltransferase activity, they add multiple mannosyl residues forming hypermannose structures, Och1p adds the initiating alpha-1,6-mannose residue to an N-linked Man8GlcNAc2 structure, the Mnn9p-containing protein complexes add further alpha-1,6-mannose residues synthesizing the backbone of the outer chain of N-linked glycans
Products: -
Products: -
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
-
Substrates: substrate specificity
Products: -
Products: -
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
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Substrates: various high mannose-type oligosaccharides as acceptors, Man8GlcNAc2-PA is the best acceptor, the loss of 1 or 2 alpha-1,2-mannoses from Man8GlcNAc2 reduces the activity
Products: -
Products: -
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
-
Substrates: substrate specificity
Products: -
Products: -
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
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Substrates: various high mannose-type oligosaccharides as acceptors, Man8GlcNAc2-PA is the best acceptor, the loss of 1 or 2 alpha-1,2-mannoses from Man8GlcNAc2 reduces the activity
Products: -
Products: -
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
-
Substrates: substrate specificity
Products: -
Products: -
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
-
Substrates: SpOch1p
Products: -
Products: -
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
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Substrates: substrate specificity
Products: -
Products: -
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
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Substrates: SpOch1p
Products: -
Products: -
?
GDP-mannose + pyridylamino-Manalpha1-3Man-alpha1-2Manalpha1-2Manalpha1-2Man
?
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Substrates: substrate for activity assay
Products: -
Products: -
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GDP-mannose + pyridylamino-Manalpha1-3Man-alpha1-2Manalpha1-2Manalpha1-2Man
?
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Substrates: substrate for activity assay
Products: -
Products: -
?
additional information
?
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Substrates: enzyme also transfers the alpha-1,6-linked branching mannose unit to the mannan of Saccharomyces cerevisiae
Products: -
Products: -
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additional information
?
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Substrates: transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
Products: -
Products: -
?
additional information
?
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Substrates: transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
Products: -
Products: -
?
additional information
?
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Substrates: enzyme also transfers the alpha-1,6-linked branching mannose unit to the mannan of Saccharomyces cerevisiae
Products: -
Products: -
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additional information
?
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Substrates: the enzyme is required for cell-wall organization and proper functioning of the secretory pathway
Products: -
Products: -
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additional information
?
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Substrates: HpOCH1 is the key enzyme responsible for initiating N-linked outer chain biosynthesis by adding the first alpha-1,6-mannose residue onto the core oligosaccharide
Products: -
Products: -
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additional information
?
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Substrates: HpOCH1 is the key enzyme responsible for initiating N-linked outer chain biosynthesis by adding the first alpha-1,6-mannose residue onto the core oligosaccharide
Products: -
Products: -
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additional information
?
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Substrates: Mnn9p, no acceptor: alpha-1,2-mannobiose
Products: -
Products: -
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additional information
?
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Substrates: Och1p adds one alpha-1,6-linked mannose residue to the core glycan of glycoproteins, e.g. pro-carboxypeptidase Y, the soluble cell wall protein Scw4p
Products: -
Products: -
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additional information
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Substrates: no acceptors for Och1p: Man5GlcNAc2 completely lacking alpha-1,2-Man, Man8GlcNAcOH
Products: -
Products: -
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additional information
?
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Substrates: Mnn9p is involved in the formation of mannan chains in the Golgi
Products: -
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additional information
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Substrates: Och1p is responsible for starting the extension of the primary N-glycans in the Golgi by addition of an alpha-1,6-mannose residue to the core glycan of glycoproteins
Products: -
Products: -
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additional information
?
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Substrates: two distinct Mnn9p-containing multi-protein complexes are responsible for the synthesis and initial branching of the long alpha-1,6-linked backbone of the hypermannose structure attached to many yeast glycoproteins, the long alpha-1,6-linked backbone is attached to an initial alpha-1,6-mannose residue transferred to the core structure by Och1p
Products: -
Products: -
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additional information
?
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Substrates: enzyme initiates outer chain formation of oligosaccharides
Products: -
Products: -
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additional information
?
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Substrates: Och1p is functional in the initiation of alpha-1,6-polymannose outer chain addition to the N-linked core oligosaccharide in yeast, Man5GlcNAc2 and Man8GlcNAc2
Products: -
Products: -
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additional information
?
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Substrates: Mnn9p is required for the addition of the long alpha-1,6-mannose backbone of the complex mannan and for the complex glycosylation of secreted proteins
Products: -
Products: -
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additional information
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Substrates: OCH1 gene encoded enzyme initiates the polymannose outer chain elongation of N-glycans, regulation of the OCH1 transcription
Products: -
Products: -
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additional information
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Substrates: involved in glycoprotein biosynthesis, enzyme catalyzes the first step specific to N-linked oligosaccharide synthesis and the biosynthesis of the outer chain of mannoproteins
Products: -
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additional information
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Substrates: Och1p is essential for the outer chain elongation of N-linked oligosaccharides
Products: -
Products: -
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additional information
?
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Substrates: the N-linked oligosaccharide modification in the Golgi apparatus is initiated by alpha1,6-mannosyltransferase (encoded by the OCH1 gene) with the addition of mannose to the Man8GlcNAc2 or Man9GlcNAc2 endoplasmic reticulum intermediates
Products: -
Products: -
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additional information
?
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Substrates: Och1p has the potential to transfer two mannoses from GDP-mannose
Products: -
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additional information
?
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Substrates: transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
Products: -
Products: -
?
additional information
?
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Substrates: both the presence and the priming activity of enzyme ScMnn9 are required for the formation of the alpha-1,6-mannose backbone of mannan proteins. Determination of the structure of the mannosyltransferase domain of ScMnn9 in complex with manganese and GDP, overview. Development of a coupled enzyme assay that involves Bacillus subtilis TN-31 aman6 (Aman6), an alpha-1,6-mannosidase, as only one additional enzyme, in contrast to the established glycosyltransferase assays where the release of GDP is measured by NADH oxidation through pyruvate kinase and lactate dehydrogenase
Products: -
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additional information
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-
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Substrates: both the presence and the priming activity of enzyme ScMnn9 are required for the formation of the alpha-1,6-mannose backbone of mannan proteins. Determination of the structure of the mannosyltransferase domain of ScMnn9 in complex with manganese and GDP, overview. Development of a coupled enzyme assay that involves Bacillus subtilis TN-31 aman6 (Aman6), an alpha-1,6-mannosidase, as only one additional enzyme, in contrast to the established glycosyltransferase assays where the release of GDP is measured by NADH oxidation through pyruvate kinase and lactate dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mnn9p is required for the addition of the long alpha-1,6-mannose backbone of the complex mannan and for the complex glycosylation of secreted proteins
Products: -
Products: -
?
additional information
?
-
Substrates: both the presence and the priming activity of enzyme ScMnn9 are required for the formation of the alpha-1,6-mannose backbone of mannan proteins. Determination of the structure of the mannosyltransferase domain of ScMnn9 in complex with manganese and GDP, overview. Development of a coupled enzyme assay that involves Bacillus subtilis TN-31 aman6 (Aman6), an alpha-1,6-mannosidase, as only one additional enzyme, in contrast to the established glycosyltransferase assays where the release of GDP is measured by NADH oxidation through pyruvate kinase and lactate dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: Och1p is functional in the initiation of alpha-1,6-polymannose outer chain addition to the N-linked core oligosaccharide in yeast, Man5GlcNAc2 and Man8GlcNAc2
Products: -
Products: -
?
additional information
?
-
-
Substrates: OCH1 gene encoded enzyme initiates the polymannose outer chain elongation of N-glycans, regulation of the OCH1 transcription
Products: -
Products: -
?
additional information
?
-
-
Substrates: no acceptors for Och1p: Man5GlcNAc2 completely lacking alpha-1,2-Man, Man8GlcNAcOH
Products: -
Products: -
?
additional information
?
-
-
Substrates: Och1p is essential for the outer chain elongation of N-linked oligosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: SpOch1p has a wider substrate specificity than ScOch1p from Saccharomyces cerevisiae
Products: -
Products: -
?
additional information
?
-
-
Substrates: SpOch1p has a wider substrate specificity than ScOch1p from Saccharomyces cerevisiae
Products: -
Products: -
?
additional information
?
-
Substrates: SpOch1p is a key enzyme in outer chain elongation of N-linked oligosaccharides on glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: SpOch1p is a key enzyme in outer chain elongation of N-linked oligosaccharides on glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is required for the initiation of outer chain elongation of N-linked oligosaccharides of cell wall mannoproteins, transcriptional control of the och1+ gene, gene expression is not regulated during the cell cycle, but is induced by salt stress through the transcription factor Atf1p
Products: -
Products: -
?
additional information
?
-
-
Substrates: SpOch1p is a key enzyme of outer chain elongation of N-linked oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is required for the initiation of outer chain elongation of N-linked oligosaccharides of cell wall mannoproteins, transcriptional control of the och1+ gene, gene expression is not regulated during the cell cycle, but is induced by salt stress through the transcription factor Atf1p
Products: -
Products: -
?
additional information
?
-
-
Substrates: SpOch1p is a key enzyme of outer chain elongation of N-linked oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in N-glycosylation pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-mannose + oligosaccharide acceptor
?
-
Substrates: Mnn9p is involved in protein mannosylation, incorporates alpha-1,6-linked mannose residues, the elongation of the N-glycan outer chain, initiated by Och1p, is continued by two mannosyltransferase complexes: V-complex composed of Mnn9p and Van1p and A-complex composed of Mnn9p, Anp1p, Hoc1p, Mnn10p and Mnn11p
Products: -
Products: -
?
additional information
?
-
-
Substrates: transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
Products: -
Products: -
?
additional information
?
-
-
Substrates: transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is required for cell-wall organization and proper functioning of the secretory pathway
Products: -
Products: -
?
additional information
?
-
Substrates: HpOCH1 is the key enzyme responsible for initiating N-linked outer chain biosynthesis by adding the first alpha-1,6-mannose residue onto the core oligosaccharide
Products: -
Products: -
?
additional information
?
-
-
Substrates: HpOCH1 is the key enzyme responsible for initiating N-linked outer chain biosynthesis by adding the first alpha-1,6-mannose residue onto the core oligosaccharide
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mnn9p is involved in the formation of mannan chains in the Golgi
Products: -
Products: -
?
additional information
?
-
-
Substrates: Och1p is responsible for starting the extension of the primary N-glycans in the Golgi by addition of an alpha-1,6-mannose residue to the core glycan of glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: two distinct Mnn9p-containing multi-protein complexes are responsible for the synthesis and initial branching of the long alpha-1,6-linked backbone of the hypermannose structure attached to many yeast glycoproteins, the long alpha-1,6-linked backbone is attached to an initial alpha-1,6-mannose residue transferred to the core structure by Och1p
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme initiates outer chain formation of oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: Och1p is functional in the initiation of alpha-1,6-polymannose outer chain addition to the N-linked core oligosaccharide in yeast, Man5GlcNAc2 and Man8GlcNAc2
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mnn9p is required for the addition of the long alpha-1,6-mannose backbone of the complex mannan and for the complex glycosylation of secreted proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: OCH1 gene encoded enzyme initiates the polymannose outer chain elongation of N-glycans, regulation of the OCH1 transcription
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in glycoprotein biosynthesis, enzyme catalyzes the first step specific to N-linked oligosaccharide synthesis and the biosynthesis of the outer chain of mannoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: Och1p is essential for the outer chain elongation of N-linked oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: the N-linked oligosaccharide modification in the Golgi apparatus is initiated by alpha1,6-mannosyltransferase (encoded by the OCH1 gene) with the addition of mannose to the Man8GlcNAc2 or Man9GlcNAc2 endoplasmic reticulum intermediates
Products: -
Products: -
?
additional information
?
-
-
Substrates: transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mnn9p is required for the addition of the long alpha-1,6-mannose backbone of the complex mannan and for the complex glycosylation of secreted proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: Och1p is functional in the initiation of alpha-1,6-polymannose outer chain addition to the N-linked core oligosaccharide in yeast, Man5GlcNAc2 and Man8GlcNAc2
Products: -
Products: -
?
additional information
?
-
-
Substrates: OCH1 gene encoded enzyme initiates the polymannose outer chain elongation of N-glycans, regulation of the OCH1 transcription
Products: -
Products: -
?
additional information
?
-
-
Substrates: Och1p is essential for the outer chain elongation of N-linked oligosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: SpOch1p is a key enzyme in outer chain elongation of N-linked oligosaccharides on glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: SpOch1p is a key enzyme in outer chain elongation of N-linked oligosaccharides on glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is required for the initiation of outer chain elongation of N-linked oligosaccharides of cell wall mannoproteins, transcriptional control of the och1+ gene, gene expression is not regulated during the cell cycle, but is induced by salt stress through the transcription factor Atf1p
Products: -
Products: -
?
additional information
?
-
-
Substrates: SpOch1p is a key enzyme of outer chain elongation of N-linked oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is required for the initiation of outer chain elongation of N-linked oligosaccharides of cell wall mannoproteins, transcriptional control of the och1+ gene, gene expression is not regulated during the cell cycle, but is induced by salt stress through the transcription factor Atf1p
Products: -
Products: -
?
additional information
?
-
-
Substrates: SpOch1p is a key enzyme of outer chain elongation of N-linked oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in N-glycosylation pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
additional information
Mn2+
-
absolute requirement, optimum concentration: 10 mM, Ca2+, Mg2+, Co2+ or Zn2+ cannot substitute for Mn2+
additional information
Ni2+, Mg2+, Ca2+, and Zn2+ cannot substitute for Mn2+
additional information
-
Ni2+, Mg2+, Ca2+, and Zn2+ cannot substitute for Mn2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
och1+ gene expression is induced by NaCl and KCl through the transcription factor Atf1p
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
A novel homozygous mutation in the human ALG12 gene results in an aberrant profile of oligomannose N-glycans in patient's serum.
Influenza, Human
Localization of a yeast early Golgi mannosyltransferase, Och1p, involves retrograde transport.
Metabolic Diseases
A novel homozygous mutation in the human ALG12 gene results in an aberrant profile of oligomannose N-glycans in patient's serum.
Tuberculosis
Characterization of a putative alpha-mannosyltransferase involved in phosphatidylinositol trimannoside biosynthesis in Mycobacterium tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.35
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
-
-
0.39
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
-
-
additional information
additional information
steady-state kinetics of wild-type ScMnn9 enzyme
-
additional information
additional information
-
steady-state kinetics of wild-type ScMnn9 enzyme
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
relative activity at 27°C 87%, at 37°C 46%, strain J-1012 alpha-1,6-MT
additional information
-
relative activity at 27°C 81%, at 37°C 27%, strain B-792 alpha-1,6-MT
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 7
-
relative activity at pH 2 28%, at pH 7 100%, strain J-1012 alpha-1,6-MT
6.5 - 8.5
-
the recombinant Och1p in Tris/malate buffer exhibits above 80% of maximum activity between pH 6.5 and pH 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Aspergillus fumigatus strain YJ-407
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme recycles between the Golgi and the endoplasmic reticulum, Och1p functions in the endoplasmic reticulum when allowed to accumulate there together with substrate proteins
brenda
-
the Mnn9p-containing multi-protein complexes cycle back and forth between the endoplasmic reticulum and Golgi, type II transmembrane protein
brenda
-
enzyme recycles between the Golgi and the endoplasmic reticulum, but normally functions in the cis-Golgi
brenda
-
Mnn9p, primarily localized to the cis Golgi, type II transmembrane protein
brenda
-
Mnn9p, cis Golgi, the Mnn9p-containing multi-protein complexes cycle back and forth between the endoplasmic reticulum and Golgi, type II transmembrane protein
brenda
ScMnn9p enzyme is a type II membrane proteins, possessing a short cytosolic N-terminal domain followed by a transmembrane domain that is required for anchoring to the Golgi membrane
brenda
-
ScMnn9p enzyme is a type II membrane proteins, possessing a short cytosolic N-terminal domain followed by a transmembrane domain that is required for anchoring to the Golgi membrane
-
brenda
-
Mnn9p is a membrane-associated protein, type II transmembrane protein
brenda
-
Mnn9p is a membrane-associated protein, type II transmembrane protein
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
the enzyme belongs to the CAZy glycosyltransferase family GT-62 that contains metal-dependent, retaining mannosyltransferases that are predicted to possess the GT-A fold and use GDP-Man as their donor substrate
evolution
-
the enzyme belongs to the CAZy glycosyltransferase family GT-62 that contains metal-dependent, retaining mannosyltransferases that are predicted to possess the GT-A fold and use GDP-Man as their donor substrate
-
malfunction
-
the variant surface glycoprotein sVSG221 synthesized by the ALG12-/- parasites shows different glycosylation patterns to that synthesized by wild-type cells, changes in sVSG221 glycosylation induced by the deletion of the ALG12 gene, overview
malfunction
cells expressing catalytically inactive ScMnn9p show growth kinetics comparable with those measured for cells lacking the enzyme, phenotypes of inactive enzyme mutants, overview
malfunction
deletion of the mnn9 gene results in an increased sensitivity to calcofluor white, Congo red, or hygromycin B as well as in reduced cell wall components and abnormal polarity. Although there is no major effect on N-glycan synthesis, covalently-linked cell wall mannoprotein Mp1 is significantly reduced in the mutant
malfunction
-
the deletion mutant DELTAVdOCH1 is impaired in certain characteristics such as fungal growth, conidia production, and microsclerotia formation. Also, DELTAVdOCH1 mutants are more sensitive to the cell wall perturbing reagents, such as SDS and Congo red, lose their penetration ability through cellophane membrane, and exhibit dramatically decreased pathogenicity to sunflower
malfunction
-
cells expressing catalytically inactive ScMnn9p show growth kinetics comparable with those measured for cells lacking the enzyme, phenotypes of inactive enzyme mutants, overview
-
malfunction
-
deletion of the mnn9 gene results in an increased sensitivity to calcofluor white, Congo red, or hygromycin B as well as in reduced cell wall components and abnormal polarity. Although there is no major effect on N-glycan synthesis, covalently-linked cell wall mannoprotein Mp1 is significantly reduced in the mutant
-
physiological function
-
the TbALG12 gene encodes the alpha1-6-mannosyltransferase that converts Man7GlcNAc2-PP-Dol to Man8GlcNAc2-PP-Dol
physiological function
ScMnn9p catalytic activity is indispensable for mannoprotein synthesis in yeast. Yeast mannan biosynthesis is initiated by a Golgi-located complex (M-Pol I) of two GT-62 mannosyltransferases, Mnn9p and Van1p, that are conserved in fungal pathogens. Enzyme Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis, an allosteric activator for ScVan1 polymerase activity
physiological function
Mnn9 is required for mannan and mannoprotein biosynthesis. The enzyme is essential for cell wall integrity, morphogenesis, and proper localization of cell wall mannoprotein
physiological function
-
the enzyme manipulates the biological characteristics, microsclerotia formation and pathogenic ability of Verticillium dahliae in sunflower
physiological function
a mutant lacking MNN9 is blocked in the earliest steps of backbone synthesis displays irregular borders and very wrinkled colony surface. Loss of MNN9 also stimulates cell wall chitin deposition
physiological function
knockdown of OCH1 significantly reduces secondary and tertiary wall thickness. Reduced OCH1 expression results in changes in thick cell wall cellulose aggregation and more apparent irregular wavy fiber bundles. Astaxanthin synthesis is not affected
physiological function
-
ScMnn9p catalytic activity is indispensable for mannoprotein synthesis in yeast. Yeast mannan biosynthesis is initiated by a Golgi-located complex (M-Pol I) of two GT-62 mannosyltransferases, Mnn9p and Van1p, that are conserved in fungal pathogens. Enzyme Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis, an allosteric activator for ScVan1 polymerase activity
-
physiological function
-
Mnn9 is required for mannan and mannoprotein biosynthesis. The enzyme is essential for cell wall integrity, morphogenesis, and proper localization of cell wall mannoprotein
-
additional information
enzyme ScMnn9 possesses the GT-A fold and shows structural similarity to GT families 15 and 78. ScMnn9 possesses a unique extrusion that may act as a molecular ruler or multimerization domain
additional information
-
enzyme ScMnn9 possesses the GT-A fold and shows structural similarity to GT families 15 and 78. ScMnn9 possesses a unique extrusion that may act as a molecular ruler or multimerization domain
additional information
-
enzyme ScMnn9 possesses the GT-A fold and shows structural similarity to GT families 15 and 78. ScMnn9 possesses a unique extrusion that may act as a molecular ruler or multimerization domain
-
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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). OCH1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
480
1
55156
Swiss-Prot
other Location (Reliability: 2)
OCH1_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
385
1
44828
Swiss-Prot
-
OCH1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
396
0
45930
Swiss-Prot
-
MNN9_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
395
0
45955
Swiss-Prot
other Location (Reliability: 1)
MNN9_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
368
0
42782
Swiss-Prot
-
Q4WIL2_ASPFU
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)
397
0
44428
TrEMBL
-
Q6C286_YARLI
Yarrowia lipolytica (strain CLIB 122 / E 150)
360
0
40356
TrEMBL
Mitochondrion (Reliability: 5)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
sequence of Anl1p contains a putative transmembrane domain, enzyme interacts with YlMnn9p
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and mutant enzymes, sitting drop vapour diffusion, mixing of 0.0005 ml of protein solution with 0.0005 ml of preciputation solution containing 0.1 M HEPES, pH 7.5, and 2 M ammonium sulfate, crystals are soaked in 50% Na-malonate, pH 7.5, containing mersalyl acid for 16 h at 20°C, crystals of ScMnn9-D236N mutant are transferred to 50% Na-malonate, pH 7.5, and soaked with 3 mM GDP and 10 mM MnCl2 for 10 min at 20°C, X-ray diffraction structure determination and analysis at 2.0-2.2 A resolution, modeling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D236N
site-directed mutagenesis, D236 is the first aspartic acid in the canonical GT-A DxD catalytic motif, and mutation to the isosteric asparagine results in the loss of activity
M16/O16
-
chimeric Mnn9p-Och1p protein, a peptide from the first to the 16th amino acids of Mnn9p is fused with a polypeptide from the 16th to the 480th amino acids of Och1p
M33/O37
-
chimeric Mnn9p-Och1p protein, a peptide from the first to the 33th amino acids of Mnn9p is fused with a polypeptide from the 37th to the 480th amino acids of Och1p
M93/O80
-
chimeric Mnn9p-Och1p protein, a peptide from the first to the 93th amino acids of Mnn9p is fused with a polypeptide from the 80th to the 480th amino acids of Och1p
D236N
-
site-directed mutagenesis, D236 is the first aspartic acid in the canonical GT-A DxD catalytic motif, and mutation to the isosteric asparagine results in the loss of activity
-
W266stop
inactive mutant strain 7X4 with a nonsense mutation resulting in a truncated Och1p, temperature- and hygromycin B-sensitive, no synthesis of outer chains on acid phosphatase
additional information
additional information
-
och1 mutants, och1 mutation causes a complete loss of the alpha-1,6-polymannose outer chain
additional information
-
DELTAmnn9 mutant with N-glycosylation defect, null mutant, chimera Mnn9 proteins
additional information
construction of a yeast DELTAMNN9 enzyme deletion strain, presence of inactive full-length ScMnn9 protein partially rescues the DELTAMNN9 phenotype
additional information
-
construction of a yeast DELTAMNN9 enzyme deletion strain, presence of inactive full-length ScMnn9 protein partially rescues the DELTAMNN9 phenotype
additional information
-
construction of a yeast DELTAMNN9 enzyme deletion strain, presence of inactive full-length ScMnn9 protein partially rescues the DELTAMNN9 phenotype
-
additional information
-
och1 mutants, och1 mutation causes a complete loss of the alpha-1,6-polymannose outer chain
-
additional information
-
och1+ gene deficient strain shows loss of mannose transfer from GDP-mannose to Man9GlcNAc2-PA and loss of high-mannose type sugar chain glycosylation, och1 mutant that does not synthesize the outer chains containing mannose on acid phosphatase
additional information
disruption mutant of och1+: viable, slow-growing phenotype, temperature- and hygromycin B-sensitive, no synthesis of outer chains on acid phosphatase
additional information
-
disruption mutant of och1+: viable, slow-growing phenotype, temperature- and hygromycin B-sensitive, no synthesis of outer chains on acid phosphatase
additional information
-
och1+ gene deficient strain shows loss of mannose transfer from GDP-mannose to Man9GlcNAc2-PA and loss of high-mannose type sugar chain glycosylation, och1 mutant that does not synthesize the outer chains containing mannose on acid phosphatase
-
additional information
-
OCH1 and Anl1 deletion strains, increased sensitivity to sodium dodecyl sulfate, and to Calcofluor White
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
particulate enzyme fractions are obtained by centrifugation of Candida albicans cell homogenates
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli BL21(DE3) pLysS by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
as a fusion with the with green fluorescent protein, MNN9-OCH1 chimeric genes are constructed and cloned
-
as a fusion with the with red fluorescent protein, MNN9-OCH1 chimeric genes are constructed and cloned
-
och1+ gene encodes alpha-1,6-mannosyltransferase, recombinant expression and cloning, och1+ gene knockout fission yeast
-
recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli BL21(DE3) pLysS, expression of mutant enzymes in Saccharomyces cerevisiae strain BY4741 DELTAMNN9
recombinant Och1p is expressed in Pichia pastoris as a secreted protein, after truncation of its transmembrane region and fusion with myc and histidine tags at the C-terminus
-
transcription of the OCH1 gene encoding alpha-1,6-mannosyltransferase is regulated by 2 transcription factors, Swi4 and Skn7, it is controlled by the ubiquitin-dependent degradation pathway
-
transcriptional control of the och1+ gene, gene expression is not regulated during the cell cycle, but is induced by NaCl and KCl through the transcription factor Atf1p
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
during the green, motile, cell stage OCH1 is stably expressed at low levels. During the thick cell wall formation stage, high levels of OCH1 expression are observed
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
along with the possibility of a lack of the immunogenic terminal alpha-1,3-mannose linkages in Yarrowia lipolytica, a Yloch1delta mutant strain can be exploited as a platform strain for developing another potential yeast system that can produce recombinant glycoproteins with human-compatible oligosaccharides
synthesis
downregulation of the mannan synthesis pathway to disrupt cell wall synthesis may simplify cell wall disruption when extracting astaxanthin
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Cloning and analysis of the Saccharomyces cerevisiae MNN9 and MNN1 genes required for complex glycosylation of secreted proteins
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Saccharomyces cerevisiae
brenda
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Reason, A.J.; Dell, A.; Romero, P.A.; Herscovics, A.
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Glycobiology
1
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1991
Saccharomyces cerevisiae
brenda
Nakanishi-Shindo, Y.; Nakayama, K.; Tanaka, A.; Toda, Y.; Jigami, Y.
Structure of the N-linked oligosaccharides that show the complete loss of alpha-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae
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268
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1993
Saccharomyces cerevisiae, Saccharomyces cerevisiae Och1p
brenda
Yamamoto, K.; Okamoto, M.; Yoko-o, T.; Jigami, Y.
Salt stress induces the expression of the Schizosaccharomyces pombe och1+, which encodes an initiation-specific alpha-1,6-mannosyltransferase for N-linked outer chain synthesis of cell wall mannoproteins
Biosci. Biotechnol. Biochem.
67
927-929
2003
Schizosaccharomyces pombe, Schizosaccharomyces pombe Och1p
brenda
Cui, Z.; Horecka, J.; Jigami, Y.
Cdc4 is involved in the transcriptional control of OCH1, a gene encoding alpha-1,6-mannosyltransferase in Saccharomyces cerevisiae
Yeast
19
69-77
2002
Saccharomyces cerevisiae, Saccharomyces cerevisiae Och1p
brenda
Tsukahara, K.; Watanabe, T.; Yokoo, T.; Chigami, Y.
Schizosaccharomyces pombe och1+ gene encoding alpha-1,6-mannosyltransferase and use of och1+ gene knockout fission yeast for production of glycoprteins with reduced glycosylation
Jpn. Kokai Tokkyo Koho
11pp
2001
Schizosaccharomyces pombe, Schizosaccharomyces pombe Och1p
-
brenda
Nakayama, K.; Nakanishi-Shindo, Y.; Tanaka, A.; Haga-Toda, Y.; Jigami, Y.
Substrate specificity of alpha-1,6-mannosyltransferase that initiates N-linked mannose outer chain elongation in Saccharomyces cerevisiae
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412
547-550
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Saccharomyces cerevisiae, Saccharomyces cerevisiae Och1p
brenda
Suzuki, A.; Shibata, N.; Suzuki, M.; Saitoh, F.; Takata, Y.; Oshie, A.; Oyamada, H.; Kobayashi, H.; Suzuki, S.; Okawa, Y.
Characterization of alpha-1,6-mannosyltransferase responsible for the synthesis of branched side chains in Candida albicans mannan
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240
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1996
Candida albicans, Candida albicans NIH B-792 serotype B
brenda
Kojima, H.; Hashimoto, H.; Yoda, K.
Interaction among the subunits of Golgi membrane mannosyltransferase complexes of the yeast Saccharomyces cerevisiae
Biosci. Biotechnol. Biochem.
63
1970-1976
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Saccharomyces cerevisiae
brenda
Jungmann, J.; Munro, S.
Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with alpha-1,6-mannosyltransferase activity
EMBO J.
17
423-434
1998
Saccharomyces cerevisiae
brenda
Yoko-o, T.; Tsukahara, K.; Watanabe, T.; Hata-Sugi, N.; Yoshimatsu, K.; Nagasu, T.; Jigami, Y.
Schizosaccharomyces pombe och1+ encodes alpha-1,6-mannosyltransferase that is involved in outer chain elongation of N-linked oligosaccharides
FEBS Lett.
489
75-80
2001
Schizosaccharomyces pombe (Q9UTR6), Schizosaccharomyces pombe
brenda
Karhinen, L.; Makarow, M.
Activity of recycling Golgi mannosyltransferases in the yeast endoplasmic reticulum
J. Cell Sci.
117
351-358
2004
Saccharomyces cerevisiae
brenda
Todorow, Z.; Spang, A.; Carmack, E.; Yates, J.; Schekman, R.
Active recycling of yeast Golgi mannosyltransferase complexes through the endoplasmic reticulum
Proc. Natl. Acad. Sci. USA
97
13643-13648
2000
Saccharomyces cerevisiae
brenda
Barnay-Verdier, S.; Boisrame, A.; Beckerich, J.M.
Identification and characterization of two alpha-1,6-mannosyltransferases, Anl1p and Och1p, in the yeast Yarrowia lipolytica
Microbiology
150
2185-2195
2004
Yarrowia lipolytica
brenda
Kitajima, T.; Chiba, Y.; Jigami, Y.
Saccharomyces cerevisiae alpha1,6-mannosyltransferase has a catalytic potential to transfer a second mannose molecule
FEBS J.
273
5074-5085
2006
Saccharomyces cerevisiae
brenda
Uccelletti, D.; Farina, F.; Rufini, S.; Magnelli, P.; Abeijon, C.; Palleschi, C.
The Kluyveromyces lactis alpha1,6-mannosyltransferase KlOch1p is required for cell-wall organization and proper functioning of the secretory pathway
FEMS Yeast Res.
6
449-457
2006
Kluyveromyces lactis
brenda
Kim, M.W.; Kim, E.J.; Kim, J.Y.; Park, J.S.; Oh, D.B.; Shimma, Y.; Chiba, Y.; Jigami, Y.; Rhee, S.K.; Kang, H.A.
Functional characterization of the Hansenula polymorpha HOC1, OCH1, and OCR1 genes as members of the yeast OCH1 mannosyltransferase family involved in protein glycosylation
J. Biol. Chem.
281
6261-6272
2006
Ogataea angusta (Q56VL2), Ogataea angusta
brenda
Song, Y.; Choi, M.H.; Park, J.N.; Kim, M.W.; Kim, E.J.; Kang, H.A.; Kim, J.Y.
Engineering of the yeast Yarrowia lipolytica for the production of glycoproteins lacking the outer-chain mannose residues of N-glycans
Appl. Environ. Microbiol.
73
4446-4454
2007
Yarrowia lipolytica
brenda
Goto, K.; Okawa, Y.
Activity and stability of alpha- and beta-mannosyltransferases in Candida albicans cells cultured at high temperature and at low pH
Biol. Pharm. Bull.
31
1333-1336
2008
Candida albicans, Candida albicans J-1012
brenda
Okamoto, M.; Yoko-o, T.; Miyakawa, T.; Jigami, Y.
The cytoplasmic region of alpha-1,6-mannosyltransferase Mnn9p is crucial for retrograde transport from the Golgi apparatus to the endoplasmic reticulum in Saccharomyces cerevisiae
Eukaryot. Cell
7
310-318
2008
Saccharomyces cerevisiae
brenda
Barnay-Verdier, S.; Beckerich, J.M.; Boisrame, A.
New components of Yarrowia lipolytica Golgi multi-protein complexes containing the alpha-1,6-mannosyltransferases YlMnn9p and YlAnl1p
Curr. Genet.
54
313-323
2008
Yarrowia lipolytica (Q6C286), Yarrowia lipolytica
brenda
Izquierdo, L.; Mehlert, A.; Ferguson, M.A.
The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases
Glycobiology
22
696-703
2012
Trypanosoma brucei
brenda
Striebeck, A.; Robinson, D.A.; Schuettelkopf, A.W.; van Aalten, D.M.
Yeast Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis
Open Biology
3
130022
2013
Saccharomyces cerevisiae (P39107), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P39107)
brenda
Zhang, J.; Zhang, Y.; Yang, J.; Kang, L.; EloRM, A.M.; Zhou, H.; Zhao, J.
The alpha-1,6-mannosyltransferase VdOCH1 plays a major role in microsclerotium formation and virulence in the soil-borne pathogen Verticillium dahliae
Fungal Biol.
123
539-546
2019
Verticillium dahliae
brenda
Du, T.; Ouyang, H.; Voglmeir, J.; Wilson, I.B.H.; Jin, C.
Aspergillus fumigatus Mnn9 is responsible for mannan synthesis and required for covalent linkage of mannoprotein to the cell wall
Fungal Genet. Biol.
128
20-28
2019
Aspergillus fumigatus (Q4WIL2), Aspergillus fumigatus, Aspergillus fumigatus ATCC MYA-4609 (Q4WIL2)
brenda
Xu, R.; Zhang, L.; Yu, W.; Liu, J.
A strategy for interfering with the formation of thick cell walls in Haematococcus pluvialis by down-regulating the mannan synthesis pathway
Bioresour. Technol.
362
127783
2022
Haematococcus lacustris (A0A699YLQ1)
brenda
Dean, N.; Jones, R.; DaSilva, J.; Chionchio, G.; Ng, H.
The Mnn10/Anp1-dependent N-linked outer chain glycan is dispensable for Candida albicans cell wall integrity
Genetics
221
221
2022
Candida albicans (P53697)
brenda
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