Information on EC 2.4.1.32 - glucomannan 4-beta-mannosyltransferase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
2.4.1.32
-
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RECOMMENDED NAME
GeneOntology No.
glucomannan 4-beta-mannosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GDP-mannose + (glucomannan)n = GDP + (glucomannan)n+1
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
GDP-mannose:glucomannan 4-beta-D-mannosyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
37257-30-0
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
var. Alaska
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
evidence is provided that AkCSLA3 is the glucomannan synthase responsible for the synthesis of storage glucomannan in corms of Amorphophallus konjac using the substrates GDP-D-mannose and GDP-D-glucose
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GDP-D-mannose + (glucomannan)n
GDP + (glucomannan)n+1
show the reaction diagram
additional information
?
-
two different types of glucomannan synthase assays, differing in the [14C]-labeled nucleotide sugar donor, are conducted: Glc-ManS (GDP-[14C]-glucose), and GlcMan-S (GDP-[14C]-mannose)
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GDP-D-mannose + (glucomannan)n
GDP + (glucomannan)n+1
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required, optimum concentration: 10 mM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
slight
Ca2+
-
above 5 mM
CHAPS
-
0.25-1%
CHAPSO
-
0.25-1%
Co2+
-
above 5 mM
CTP
-
slight
cyclohexandione
-
slight inactivation
Digitonin
-
slightly inhibitory at 1%
formaldehyde
-
46% inactivation at 10 mM in presence of NaCNBH3
GDP-D-glucose
GDP-L-fucose
-
40% inhibition at 1 mM
glycerol
Mg2+
-
slightly inhibitory at 1-15 mM
Mn2+
-
strong inhibition at 5 mM
N-ethylmaleimide
-
concentration-dependent inactivation
Phenylglyoxal
-
concentration and time-dependent
Phosphate buffer
-
slight
-
Phospholipase A2
-
fast inactivation, irreversible
-
Phospholipase C
-
slow inactivation, irreversible
-
Triton X-100
-
0.25-1%
UDP
-
slight
UTP
-
slight
additional information
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
not affected by spermine, spermidine, cellobiose, tunicamycin, bacitracin, EDTA and EGTA
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.182
GDP-D-mannose
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.006
GDP-D-glucose
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0017
-
membrane-bound and digitonin-solubilized enzyme
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
pH 6.5: 55% of activity maximum, pH 9.0: 10% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
30% remaining activity at 2�C; cold-stress does not alter enzyme activity
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
differentiated and differentiating cells
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.32)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)