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Information on EC 5.3.1.8 - mannose-6-phosphate isomerase and Organism(s) Candida albicans and UniProt Accession P34948
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5.3.1.8 mannose-6-phosphate isomeraseIUBMB Comments
A zinc protein.
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Word Map
- 5.3.1.8
- phosphomannomutase
- gdp-mannose
-
pyrophosphorylase
- phosphoglucomutase
- fructose-6-phosphate
-
phosphoglucose
- enteropathy
-
carbohydrate-deficient
- viannia
-
allozyme
- braziliensis
- chlorophenol
-
mannose-containing
-
man-6-p
- phosphoglucoisomerase
-
biolistic
-
protein-losing
- l-ribose
- peruviana
- synthesis
- thermodenitrificans
-
guyanensis
- biotechnology
- agriculture
- pharmacology
- analysis
The taxonomic range for the selected organisms is: Candida albicans
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphomannose isomerase, mannose phosphate isomerase, mannose-6-phosphate isomerase, phosphohexoisomerase, phosphomannoisomerase, phosphomannose-isomerase, phosphohexomutase, gtmpi, type i phosphomannose isomerase, type i pmi, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-mannose-6-phosphate ketol-isomerase
-
-
-
-
Isomerase, mannose phosphate
-
-
-
-
Mannose phosphate isomerase
-
-
-
-
Phosphohexoisomerase
-
-
-
-
Phosphohexomutase
-
-
-
-
Phosphomannoisomerase
-
-
-
-
Phosphomannose isomerase
-
-
-
-
Phosphphexomutase
-
-
-
-
PMI
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-mannose-6-phosphate aldose-ketose-isomerase
A zinc protein.
CAS REGISTRY NUMBER
COMMENTARY
9023-88-5
-
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
additional information
?
-
-
enzyme is involved in biosynthesis of mannan components of the cell walls
-
-
?
additional information
?
-
-
enzyme is involved in biosynthesis of mannan components of the cell walls
-
-
?
additional information
?
-
-
reversible isomerization of mannose 6-phosphate and fructose 6-phosphate is the initial commited step in the synthesis of the mannosylated glycoproteins, which are essential in biosynthesis of functional fungal cell wall. Absence of mannose-6-phosphate isomerase causes cell lysis
-
-
?
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
additional information
?
-
-
enzyme is involved in biosynthesis of mannan components of the cell walls
-
-
?
additional information
?
-
-
enzyme is involved in biosynthesis of mannan components of the cell walls
-
-
?
additional information
?
-
-
reversible isomerization of mannose 6-phosphate and fructose 6-phosphate is the initial commited step in the synthesis of the mannosylated glycoproteins, which are essential in biosynthesis of functional fungal cell wall. Absence of mannose-6-phosphate isomerase causes cell lysis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
The Zn binding mode of the 5-phospho-D-arabinonhydrazide inhibitor mimics the bidentate Zn coordination of substrate and high energy intermediate
Zinc
Zinc
-
recombinant enzyme expressed in E. coli contains slightly less than 1 mol of zinc per mol of proteins
Zinc
-
enzyme contains an essential zinc atom. Four of the five ligands come from the protein, one of these ligands is unique in that it is a glutamine
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ag+
-
irreversible inhibition in a two-step process, mannose 6-phosphate protects against inactivation. Mutant enzyme Cys150Ala shows 1000fold less sensitivity than the wild-type enzyme
Silver sulfadiazine
-
wild-type enzyme is inhibited, mutant enzyme Cys150Ala is not inhibited
Hg2+
-
partial noncompetitive inhibition with mannose 6-phosphate as substrate. In addition to the inhibition at rapid equilibrium, inactivation occurs in a two-step process, proceeding via an intermediate complex. The rate of the irreversible inactivation can be slowed by the addition of the substrate mannose 6-phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
D-mannose 6-phosphate
pH not specified in the publication, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
5-phospho-D-arabinonhydrazide
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
49060
-
selenomethionine-labelled enzyme expressed in E. coli, electrospray mass spectroscopy
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure complexed with inhibitor 5-phospho-D-arabinonhydrazide at 1.85 A resolution. Glu294 is the catalytic base that transfers a proton between the C1 and C2 carbon atoms of the substrate. The inhibitor shows bidentate coordination
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C150A
-
mutant Cys150Ala shows similar Km-values and maximal velocity as compared to the wild-type enzyme. The mutant enzyme shows no inhibition by silver sulfadiazine, and is 1000fold less sensitive to Hg2+ inhibition
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and selenomethionine-labelled enzyme expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
-
absence of mannose-6-phosphate isomerase causes cell lysis and thus the enzyme is a potential target for inhibition and may be a route to antifungal drugs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wells, T.N.C.; Payton, M.A.; Proudfoot, A.E.I.
Inhibition of phosphomannose isomerase by mercury ions
Biochemistry
33
7641-7646
1994
Saccharomyces cerevisiae, Candida albicans, Homo sapiens, Sus scrofa
Wells, T.N.C.; Scully, P.; Paravicini, G.; Proudfoot, A.E.I.; Payton, M.A.
Mechanism of irreversible inactivation of phosphomannose isomerase by silver ions and flamazine
Biochemistry
34
7896-7903
1995
Candida albicans, Escherichia coli
Tolley, S.; Davies, G.; Hubbard, R.E.; Smith, D.J.; Proudfoot, A.E.I.; Payton, M.A.; Cleasby, A.; Wonacott, A.; Wells, T.N.C.
Crystallization and preliminary X-ray analysis of Candida albicans phosphomannose isomerase
J. Mol. Biol.
237
349-350
1994
Candida albicans
Cleasby, A.; Wonacott, A.; Skarzynski, T.; Hubbard, R.E.; Davies, G.J.; Proudfoot, A.E.I.; Bernard, A.R.; Payton, M.A.; Wells, T.N.C.
The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 A resolution
Nat. Struct. Biol.
3
470-479
1996
Candida albicans
Bernard, A.R.; Wells, T.N.C.; Cleasby, A.; Borlat, F.; Payton, M.A.; Proufoot, A.E.I.
Selenomethionine labelling phosphomannose isomerase changes its kinetic properties
Eur. J. Biochem.
230
111-118
1995
Candida albicans
Proudfoot, A.E.I.; Payton, M.A.; Wells, N.C.
Purification and characterization of fungal and mammalian phosphomannose isomerases
J. Protein Chem.
13
619-627
1994
Saccharomyces cerevisiae, Candida albicans, Homo sapiens, Sus scrofa
Ahmad, L.; Plancqueel, S.; Dubosclard, V.; Lazar, N.; Ghattas, W.; Li de la Sierra-Gallay, I.; van Tilbeurgh, H.; Salmon, L.
Crystal structure of phosphomannose isomerase from Candida albicans complexed with 5-phospho-D-arabinonhydrazide
FEBS Lett.
592
1667-1680
2018
Candida albicans (P34948), Candida albicans ATCC MYA-2876 (P34948)
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