Information on EC 2.4.1.34 - 1,3-beta-glucan synthase

New: Word Map on EC 2.4.1.34
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.4.1.34
-
RECOMMENDED NAME
GeneOntology No.
1,3-beta-glucan synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + [(1->3)-beta-D-glucosyl]n = UDP + [(1->3)-beta-D-glucosyl]n+1
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,3-beta-D-glucan biosynthesis
-
-
Starch and sucrose metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:(1->3)-beta-D-glucan 3-beta-D-glucosyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9037-30-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC31749, expression in Agrobacterium or Escherichia coli
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Col-0
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
sugar beet
-
-
Manually annotated by BRENDA team
cauliflower
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Christm. Swing., mexican lime
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Fusarium solani f.sp.pisi
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
french bean
-
-
Manually annotated by BRENDA team
subsp. patens, 12 putative callose synthase genes, PpCalS1-PpCalS10
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucose + (1,3-beta-D-glucosyl)n
UDP + (1,3-beta-D-glucosyl)n+1
show the reaction diagram
UDP-glucose + [(1,3)-beta-D-glucosyl]n
UDP + [(1,3)-beta-D-glucosyl]n+1
show the reaction diagram
UDPglucose + (1,3-beta-D-glucosyl)n
UDP + (1,3-beta-D-glucosyl)n+1
show the reaction diagram
additional information
?
-
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
UDP-glucose + [(1,3)-beta-D-glucosyl]n
UDP + [(1,3)-beta-D-glucosyl]n+1
show the reaction diagram
UDPglucose + (1,3-beta-D-glucosyl)n
UDP + (1,3-beta-D-glucosyl)n+1
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Sr2+
-
stimulates, less effective than Ca2+
additional information
-
no requirement for metal cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,3R,6aS,7R,8R,10bR,12aR)-1,6a,8,10a-tetramethyl-8-[(2R)-3-methylbutan-2-yl]-2-[[(2R)-1-methylpyrrolidin-2-yl]methoxy]-3-[5-(pyridin-4-yl)-1H-1,2,4-triazol-1-yl]-1,3,4,6,6a,7,8,9,10,10a,10b,11,12,12a-tetradecahydro-2H-1,4a-(methanooxymethano)chrysene-7-carboxylic acid
-
IC50: 19 ng/ml, pH and temperature not specified in the publication
(1R,3R,6aS,7R,8R,10bR,12aR)-1,6a,8,10a-tetramethyl-8-[(2R)-3-methylbutan-2-yl]-2-[[(2R)-2-methylpyrrolidin-2-yl]methoxy]-3-[5-(pyridin-4-yl)-1H-1,2,4-triazol-1-yl]-1,3,4,6,6a,7,8,9,10,10a,10b,11,12,12a-tetradecahydro-2H-1,4a-(methanooxymethano)chrysene-7-carboxylic acid
-
IC50: 4 ng/ml, pH and temperature not specified in the publication
(1R,3R,6aS,7R,8R,10bR,12aR)-1,6a,8,10a-tetramethyl-8-[(2R)-3-methylbutan-2-yl]-2-[[(2S)-1-methylpyrrolidin-2-yl]methoxy]-3-[5-(pyridin-4-yl)-1H-1,2,4-triazol-1-yl]-1,3,4,6,6a,7,8,9,10,10a,10b,11,12,12a-tetradecahydro-2H-1,4a-(methanooxymethano)chrysene-7-carboxylic acid
-
IC50: 61 ng/ml, pH and temperature not specified in the publication
(1R,3R,6aS,7R,8R,10bR,12aR)-1,6a,8,10a-tetramethyl-8-[(2R)-3-methylbutan-2-yl]-3-[5-(pyridin-4-yl)-1H-1,2,4-triazol-1-yl]-2-[(2R)-pyrrolidin-2-ylmethoxy]-1,3,4,6,6a,7,8,9,10,10a,10b,11,12,12a-tetradecahydro-2H-1,4a-(methanooxymethano)chrysene-7-carboxylic acid
-
IC50: 22 ng/ml, pH and temperature not specified in the publication
(1R,3R,6aS,7R,8R,10bR,12aR)-1,6a,8,10a-tetramethyl-8-[(2R)-3-methylbutan-2-yl]-3-[5-(pyridin-4-yl)-1H-1,2,4-triazol-1-yl]-2-[(2S)-pyrrolidin-2-ylmethoxy]-1,3,4,6,6a,7,8,9,10,10a,10b,11,12,12a-tetradecahydro-2H-1,4a-(methanooxymethano)chrysene-7-carboxylic acid
-
IC50: 18 ng/ml, pH and temperature not specified in the publication
(1R,3R,6aS,7R,8R,10bR,12aR)-2-[[(2R)-1,2-dimethylpyrrolidin-2-yl]methoxy]-1,6a,8,10a-tetramethyl-8-[(2R)-3-methylbutan-2-yl]-3-[5-(pyridin-4-yl)-1H-1,2,4-triazol-1-yl]-1,3,4,6,6a,7,8,9,10,10a,10b,11,12,12a-tetradecahydro-2H-1,4a-(methanooxymethano)chrysene-7-carboxylic acid
-
IC50: 6.4 ng/ml, pH and temperature not specified in the publication
(1R,6aS,7R,8R,10bR,12aR)-1,6a,8,10a-tetramethyl-8-[(2R)-3-methylbutan-2-yl]-3-[5-(pyridin-4-yl)-1H-1,2,4-triazol-1-yl]-2-[[(2R)-2,3,3-trimethyl-2-(methylamino)butyl]oxy]-1,3,4,6,6a,7,8,9,10,10a,10b,11,12,12a-tetradecahydro-2H-1,4a-(methanooxymethano)chrysene-7-carboxylic acid
-
IC50: 2 ng/ml, pH and temperature not specified in the publication
(2,6-difluoro-phenyl)-carbamic acid 3-(4-benzothiazol-2-yl-piperazine-1-yl)-propyl ester
-
The piperazine propanol derivative GS1578 was identified as a potent inhibitor against 1,3-beta-D-glucan synthase, IC50: 0.16 microM.
1,2-Bis(O-aminophenoxy)ethane-N,N,N',N'-tetraacetate
-
-
5-azido-UDP-glucose
-
-
8-hydroxyquinoline
-
-
Acylcarnitine
-
inhibition in presence of digitonin, stimulation in absence of digitonin within a certain concentration range
aerothrinicin 1
-
-
anidulafungin
-
an antifungal echinocandin drug, inhibition profile of wild-type and mutant enzymes
-
caspofungin
Caspofungin acetate
cilofungin
Congo red
-
non competitive
D-glucono-1,5-lactone
-
-
dihydrosphingosine
-
non-competitive inhibition
diphosphate
-
-
Echinocandin B
enfumafungin
-
IC50: 40 microgram/ml, pH 7.5, temperature not specified
ethanol
Glycylglycine buffer
-
0.75 M
lysophosphatidylcholine
-
inhibition in presence of digitonin, stimulation in absence of digitonin within a certain concentration range
Mg2+
-
1,3-beta-glucan synthase 1
micafungin
-
an antifungal echinocandin drug, inhibition profile of wild-type and mutant enzymes
-
MK 991
monomeric single-chain variable fragment (scFv)
N-ethylmaleimide
Natural inhibitor in green Euglena cells
-
-
-
Nonidet P-40
-
-
octylglucoside
-
-
orizabin IX
-
IC50: 0.181 mg/ml
orizabin V
-
IC50: 0.155 mg/ml
orizabin X
-
IC50: 0.070 mg/ml
orizabin XI
-
IC50: 0.072 mg/ml
orizabin XIV
-
IC50: 0.074 mg/ml
-
orizabin XIX
-
IC50: 0.062 mg/ml
orizabin XV
-
IC50: 0.149 mg/ml
orizabin XVII
-
IC50: 0.078 mg/ml
orizabin XX
-
IC50: 0.065 mg/ml
oryzalin
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
papulacandin
-
IC50: 0.02 microgram/ml, pH 7.5, temperature not specified
papulacandin B
phosphoenolpyruvate
-
-
Phospholipase A2
-
fatty acids and lysophospholipids are the inhibitory moieties
-
Phospholipase C
-
fatty acids and lysophospholipids are the inhibitory moieties
-
phytosphingosine
-
non-competitive inhibition
platelet-activating factor
-
inhibition in presence of digitonin, stimulation in absence of digitonin within a certain concentration range
pneumocandin
-
IC50: 120 microgram/ml, pH 7.5, temperature not specified
Showdomycin
Sirofluor
-
fluorochrome from aniline blue
-
TDPglucose
-
-
tricolorin A
-
IC50: 0.085 mg/ml
tricolorin B
-
IC50: 0.132 mg/ml
tricolorin C
-
IC50: 0.135 mg/ml
tricolorin D
-
IC50: 0.087 mg/ml
tricolorin E
-
IC50: 0.099 mg/ml
tricolorin F
-
IC50: more than 0.250 mg/ml
tricolorin I
-
IC50: 0.106 mg/ml
Triton X-100
unsaturated fatty acids
-
trienoic acids most effective
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-[(cholamidopropyl)dimethyl(ammonio)]propanesulfonate
-
stimulate
Acylcarnitine
-
inhibition in presence of digitonin, stimulation in absence of digitonin within a certain concentration range
alamethicin
beta-furfuryl-beta-D-glucoside
-
stimulation
beta-linked glucosides
-
stimulate
beta-methyl-D-glucoside
-
stimulate
bovine serum albumin
CaCl2
-
7 mM, 2fold increase in activity
cellobiose
cellobiosylglucose
-
stimulate
CHAPS
-
pollen CalS isozyme is activated in vitro by the detergent CHAPS, but activation is not associated with a detectable change in the molecular mass of the NaGSL1 polypeptide
cytochalasin
-
slightly activating
-
D-glucose
D-Glucosides
Digitonin
-
stimulate
Echinocandin B
-
inhibition in presence of digitonin, stimulation in absence of digitonin within a certain concentration range
EDTA
-
maximal activity at 50 mM
gentiobiose
glycerol
-
stimulate
hydroquinone-beta-D-glucoside
-
stimulate
laminaribiose
lysophosphatidylcholine
-
inhibition in presence of digitonin, stimulation in absence of digitonin within a certain concentration range
maltose
MgCl2
-
5 mM, 3fold increase in activity
platelet-activating factor
-
inhibition in presence of digitonin, stimulation in absence of digitonin within a certain concentration range
Polyamines
-
stimulate
-
Polyols
Salicin
-
stimulate
spermine
Sucrose
-
stimulate
Trypsin
-
pollen CalS isozyme, in contrast to the somatic isozyme, is activated in vitro by the proteolytic enzyme trypsin, but activation is not associated with a detectable change in the molecular mass of the NaGSL1 polypeptide. Some CalS activity is lost with longer incubations with trypsin
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21
UDP-glucose
-
pH 7.75
0.36 - 7.1
UDPglucose
0.1 - 0.13
[(1,3)-beta-D-glucosyl]n
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00217 - 0.717
UDPglucose
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00017 - 0.0041
caspofungin
0.022
cilofungin
-
pH 7.75, 25C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00016
(2,6-difluoro-phenyl)-carbamic acid 3-(4-benzothiazol-2-yl-piperazine-1-yl)-propyl ester
Candida albicans
-
The piperazine propanol derivative GS1578 was identified as a potent inhibitor against 1,3-beta-D-glucan synthase, IC50: 0.16 microM.
0.00003
Caspofungin acetate
Aspergillus fumigatus
-
IC50: 30nM
additional information
additional information
Candida glabrata
-
inhibitory potency of antifungal echinocandin drugs on different wild-type and on mutant strains, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00054
-
isoenzyme DELTAgns1
0.00126
-
-
0.00292
-
wild-type
0.0041
-
with polyoxyethylene ether in the assay but not during cell breakage
0.0048
0.0096
-
membrane plus W-1
0.0109
-
solubilized
0.0125
-
with polyoxyethylene ether in the assay and during cell breakage
0.0584
-
wild-type without GTP
0.0776
-
MAN-04 mutant without GTP
0.0924
-
wild-type with GTPgammaS
0.105
-
MAN-04 with GTPgammaS
0.11
-
RCP-3 mutant without GTP
0.33
-
RCP-3 mutant with GTPgammaS
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
-
1,3-beta-glucan synthase 1
7.2 - 7.6
-
-
8.8
-
1,3-beta-glucan synthase 2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
6.5 and 9: about 30% of activity maximum
6.8
-
optimal conditions for callose synthese in vitro
6.8 - 8.8
-
6.8 and 8.8: about 50% of activity maximum
7 - 7.8
-
7: about 60% of activity maximum, 7.8: about 70% of activity maximum
7.5 - 8.5
-
pH 7.5: activity maximum, pH 8.5: about 50% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 37
-
assay at, wild-type and temperature-sensitive mutants
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 45
-
0C: 16% of activity maximum, 37C: 44% of activity maximum, 45C: 6% of activity maximum
17 - 37
-
17C: 80% of activity maximum, 30C: 90% of activity maximum, 37C: 80% of activity maximum
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
budding and filamentous
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
-
mainly in the apical part
Manually annotated by BRENDA team
-
somatic isozyme
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
inactive, latent enzyme form
Manually annotated by BRENDA team
-
inactive, latent enzyme form
Manually annotated by BRENDA team
additional information
-
predominantly in the endoplasmic reticulum and Golgi membranes in younger pollen tubes mostly in an inactive, latent enzyme form, the latent and active enzyme forms together In later stages of pollen-tube growth to a greater proportion located in intracellular vesicles and the plasma membrane
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
PAGE
57000
-
recombinant protein
58940
-
calculated from nucleotide sequence
220000
-
pollen isozyme
221700
-
calculated from cDNA
229000
-
calculated from nucleotide sequence
420000
-
PAGE
additional information
-
in BY-2 cells, callose synthase appears in two different protein complexes with masses of approximately 1500 kDa and at 800 kDa, each co-migrating with tubulin
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
polymer
-
x * 28000, pollen isozyme, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
two distinct N- and C-terminal halves, similar in size and topology and separated by a deep cleft, both domains contain a similar core structure of parallel beta sheets connected by alpha helices, the C-terminal structure contains a glycine fingerprint sequence
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28
-
2 h, 90% loss of activity
30
-
half life without polyoxyethylene ether in the assay but during cell breakage: 11.8 h; half life without polyoxyethylene ether in the assay but not during cell breakage: 0.5 h; half life with stabilizing polyoxyethylene ether in the assay and during cell breakage: 18.4 h; half life with stabilizing polyoxyethylene ether in the assay but not during cell breakage: 15.9 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin protects against inactivation by phospholipase A2, C and papulacandin B
-
EDTA protects against inactivation by phospholipase A2 and C
-
guanosine nucleotides prevent inactivation at 30C
human serum albumin protects against inactivation by phospholipase A2, C and papulacandin B
-
inactivation at 30C is greatly accelerated by the presence of 1-2 mM EDTA
polyoxyethylene ether stabilizes the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-14C, 2 weeks, 20% loss of activity
-
-20C, 50 mM Tris-HCl, pH 7.4, 1% digitonin, 0.01% 2-mercaptoethanol, 20% sucrose or glycerol, stable for at least 1 week, losing less than 10% of initial activity
-
-70C, more than 25 weeks 100% activity
-
-70C, more than 26 weeks 100% activity
-
-80C, several months
-80C, solubilized enzyme stable for 8 h
-
4C, solubilized enzyme stable for 4 h
-
frozen, 60% loss of activity after 3 days
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
determination of expression pattern of upstream regulatory sequence of the 12 callose synthase genes, CalS112
-
eight different putative callose synthase genes, expression analysis
-
expressed in Escherichia coli
-
expression in Escherichia coli
-
expression in Neurospora crassa cell-wall-less mutant TM1
-
expression in tobacco BY2 cells
-
gene PpCalS, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis
-
genes HvGSL2-HvGSL7, mapped to individual loci that are distributed across the barley genome on chromosomes 3H, 4H, 6H and 7H, transcription patterns by quantitative real-time PCR, overview; genes HvGSL2-HvGSL7, mapped to individual loci that are distributed across the barley genome on chromosomes 3H, 4H, 6H and 7H, transcription patterns by quantitative real-time PCR, overview; genes HvGSL2-HvGSL7, mapped to individual loci that are distributed across the barley genome on chromosomes 3H, 4H, 6H and 7H, transcription patterns by quantitative real-time PCR, overview; genes HvGSL2-HvGSL7, mapped to individual loci that are distributed across the barley genome on chromosomes 3H, 4H, 6H and 7H, transcription patterns by quantitative real-time PCR, overview; genes HvGSL2-HvGSL7, mapped to individual loci that are distributed across the barley genome on chromosomes 3H, 4H, 6H and 7H, transcription patterns by quantitative real-time PCR, overview; genes HvGSL2-HvGSL7, mapped to individual loci that are distributed across the barley genome on chromosomes 3H, 4H, 6H and 7H, transcription patterns by quantitative real-time PCR, overview
genotyping
-
mushroom Cordyceps militaris beta-1,3-glucan synthase catalytic subunit Fks1 is expressed as a fusion protein with an N-terminal hexahistidine tag and glutathione S-transferase in an Escherichia coli cell-free translation system
-
the catalytic module of CrdS (cm-CrdS) is expressed in good yield from a cDNA encoding cm-CrdS cloned into a vector, containing a coding region for thioredoxin, and from the Champion pET SUMO system that possesses a coding region of a small ubiquitin-related modifier (SUMO) partner protein. The two DNA fusions are expressed as chimeric proteins. High yields of inclusion bodies are produced in Escherichia coli and these could be refolded to form soluble proteins, using a range of buffers and non-detergent sulfobetaines
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
dissociation is detected between the expression of the PbFKS1 transcript and the level of the corresponding protein PbFks1p, which is higher in the yeast phase, versus the amount of 1,3-beta-D-glucan polymer, which is higher in the mycelium phase
-
five CalS genes are differentially induced bysalicylic acid or by infection with the pathogen Hyaloperonospora arabidopsis, i.e. Peronospora parasitica, overview
-
the bird cherry-oat aphid, BCA, Rhopalosiphum padi gives no visible symptom and induces very limited callose deposition, even after 14 days of infestation. In contrast, the Russian wheat aphid, RWA, Diuraphis noxia, which causes chlorosis,white and yellowstreaking and leaf rolling, induces callose accumulation already after 24 h in longitudinal leaf veins
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A1895G
-
mutation of Fks1p
D632E
-
mutation of Fks1p
D632G
-
mutation of Fks1p
D632Y/R1377STOP
-
mutation of Fks2p and Fks1p
D666E
-
mutation of Fks2p
D666G
-
mutation of Fks2p
F625S
-
mutation of Fks1p
F659del
-
mutation of Fks2p
F659S
-
mutation of Fks2p
F659V
-
mutation of Fks2p
G1894T
-
mutation of Fks1p
P667T
-
mutation of Fks2p
S629P
-
mutation of Fks1p
S663P
-
mutation of Fks2p
T1874C
-
mutation of Fks1p
T1885C
-
mutation of Fks1p
T1896G
-
mutation of Fks1p
W1375L
-
mutation of Fks2p
DELTAgns1
-
one-fifth of the specific activity of the wild type
D13A
-
lower turnover and lower Km than wild-type
D332A
-
lower turnover and higher Km than wild-type
H125A
-
higher turnover and lower Km than wild-type
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
silencing of enzyme genes GSL5, GSL6, GSL11 with RNAi: both wound callose and papillary callose are absent in lines transformed with GSL5 dsRNAi, but unaffected in GSL6 and GSL11 RNAi lines. Absence of callose in palpillae or haustorial complexes correlates with effective growth cessation of several normally virulent powdery mildew species and of Peronospora parasitica
analysis
-
simple and sensitive method for characterization of enzyme products by analysis of newly synthesized polysaccharides by 13C-nuclear magnetic resonance
Show AA Sequence (125 entries)
Please use the Sequence Search for a certain query.