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Information on EC 2.4.1.109 - dolichyl-phosphate-mannose-protein mannosyltransferase and Organism(s) Candida albicans and UniProt Accession Q5ACU3
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2.4.1.109 dolichyl-phosphate-mannose-protein mannosyltransferaseIUBMB Comments
The enzyme transfers mannosyl residues to the hydroxy group of serine or threonine residues, producing cell-wall mannoproteins. It acts only on long-chain alpha-dihydropolyprenyl derivatives, larger than C35.
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Word Map
- 2.4.1.109
- muscular
- dystrophy
-
o-mannosylation
-
walker-warburg
- alpha-dystroglycan
- pomgnt1
-
o-glycosylation
-
fukutin
- muscle-eye-brain
- dystroglycanopathies
-
dystroglycan
-
girdle
-
alpha-dystroglycanopathy
- lissencephaly
-
fukuyama
-
hypoglycosylation
-
limb-girdle
-
alpha-dg
-
pomts
-
cobblestone
- heterotopia
-
fukutin-related
- medicine
- gmppb
-
o-mannose
- agriculture
- diagnostics
The taxonomic range for the selected organisms is: Candida albicans
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
=
+
+
=
+
Synonyms
pomt1, pomt2, protein o-mannosyltransferase, pmt1p, o-mannosyltransferase, protein o-mannosyltransferase 1, pmt2p, pmt1p-pmt2p, pmt4p, protein o-mannosyltransferase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dolichol phosphomannose-protein mannosyltransferase
-
-
-
-
mannosyltransferase, dolichol phosphomannose-protein
-
-
-
-
PMT2
PMT4
protein O-D-mannosyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
dolichyl-phosphate-D-mannose:protein O-D-mannosyltransferase
The enzyme transfers mannosyl residues to the hydroxy group of serine or threonine residues, producing cell-wall mannoproteins. It acts only on long-chain alpha-dihydropolyprenyl derivatives, larger than C35.
CAS REGISTRY NUMBER
COMMENTARY
74315-99-4
-
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
dolichyl phosphate D-mannose + Ac-Ala-Thr-Ala-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Ala-Thr-Ala-NH2
-
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Ala-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Pro-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Pro-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Ala-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Ala-Thr-Ala-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Leu-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Leu-Thr-Ala-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Pro-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Pro-Thr-Ala-Val
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
-
PMT4 is required for full virulence of Candida albicans
-
-
?
additional information
?
-
-
PMT5 does not make a significant contribution to virulence
-
-
?
additional information
?
-
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
-
protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
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
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
-
PMT4 is required for full virulence of Candida albicans
-
-
?
additional information
?
-
-
PMT5 does not make a significant contribution to virulence
-
-
?
additional information
?
-
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
-
protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 8
-
the best buffers are bicine pH 7.7, tricine pH 8.0 and HEPES pH 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
Pmt proteins may be suitable targets for future novel classes of antifungal agents
medicine
-
protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans. Inhibition may prevent surface anchoring and biofilm-dependent resistance of fungal pathogens
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arroyo-Flores, B.L.; Calvo-Mendez, C.; Flores-Carreon, A.; Lopez-Romero, E.
Biosynthesis of glycoproteins in Candida albicans: activity of dolichol phosphate mannose synthase and protein mannosylation in a mixed membrane fraction
Microbiology
141
2289-2294
1995
Candida albicans
-
Weston, A.; Nassau, P.M.; Henley, C.; Marriott, M.S.
Protein O-mannosylation in Candida albicans. Determination of the amino acid sequences of peptide acceptors for protein O-mannosyltransferase
Eur. J. Biochem.
215
845-849
1993
Candida albicans, Candida albicans 2005 E
Arroyo-Flores, B.L.; Calvo-Mendez, C.; Flores-Carreon, A.; Lopez-Romero, E.
Partial purification and characterization of a mannosyltransferase involved in O-linked mannosylation of glycoproteins in Candida albicans
Antonie van Leeuwenhoek
85
199-207
2004
Candida albicans
Peltroche-Llacsahuanga, H.; Goyard, S.; dEnfert, C.; Prill, S.K.; Ernst, J.F.
Protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans
Antimicrob. Agents Chemother.
50
3488-3491
2006
Candida albicans
Rouabhia, M.; Schaller, M.; Corbucci, C.; Vecchiarelli, A.; Prill, S.K.; Giasson, L.; Ernst, J.F.
Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases
Infect. Immun.
73
4571-4580
2005
Candida albicans, Candida albicans (O74189), Candida albicans (Q59X23), Candida albicans (Q5ADM9), Candida albicans (Q9UVB5)
Prill, S.K.; Klinkert, B.; Timpel, C.; Gale, C.A.; Schroeppel, K.; Ernst, J.F.
PMT family of Candida albicans: five protein mannosyltransferase isoforms affect growth, morphogenesis and antifungal resistance
Mol. Microbiol.
55
546-560
2005
Candida albicans
Lengeler, K.B.; Tielker, D.; Ernst, J.F.
Protein-O-mannosyltransferases in virulence and development
Cell. Mol. Life Sci.
65
528-544
2008
Candida albicans (O74189), Candida albicans (Q59X23), Candida albicans (Q5ACU3), Candida albicans (Q5ADM9), Candida albicans (Q9UVB5), Cryptococcus neoformans, Mycobacterium tuberculosis, Saccharomyces cerevisiae (P31382), Saccharomyces cerevisiae (P33775), Saccharomyces cerevisiae (P42934), Saccharomyces cerevisiae (P46971), Saccharomyces cerevisiae (P47190), Saccharomyces cerevisiae (P52867), Saccharomyces cerevisiae (Q06644), Schizosaccharomyces pombe (O13898), Schizosaccharomyces pombe (O42933), Schizosaccharomyces pombe (Q9C100)
EXTERNAL LINKS (specific for EC-Number 2.4.1.109)
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