Information on EC 2.4.1.B3 - alpha-1,4-glucan synthase

Word Map on EC 2.4.1.B3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
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...)
Please login to have access to the AMENDA and FRENDA data

The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
2.4.1.B3
preliminary BRENDA-supplied EC number
top print hide
RECOMMENDED NAME
GeneOntology No.
alpha-1,4-glucan synthase
-
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + [alpha-D-glucosyl-(1-3)]n = UDP + alpha-1,4-glucosyl-[alpha-D-glucosyl-(1-3)]n
show the reaction diagram
top print hide
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:alpha-D-(1-3)-glucan alpha-(1-4)-glucosyltransferase
-
top
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
study deals with the intracellular domain of the protein
UniProt
Manually annotated by BRENDA team
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
top print hide
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
additional information
?
-
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
265000
x * 265000, SDS-PAGE
272106
x * 272106, calculated from the deduced amino acid sequence
274335
x * 274335, calculated
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of native and E1526A mutant enzyme in Schizosaccharomyces pombe, overexpression of native but not mutant enzyme results in accumulation of (1,4)-alpha-glucan
top print hide
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
mRNAs levels of Ras homology GTPase RHO2 and enzyme gene AGS1 keep a direct relationship but the levels of Ras homology GTPase RHO1 and beta-1,3-glucan synthase FKS1 do not. Growth of cells in the Y phase in YPG medium supplemented with 5% horse serum leads to an increase in the alpha-1,3-glucan content of the cell wall, without signifi cant increase in AGS1 expression, regardless of the Y cells being grown in the presence or absence of horse serum
top print hide
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA1118-1689
enzyme is not able to synthesize alpha-1,4-glucan
DELTA113-724
enzyme is able to synthesize alpha-1,4-glucan
E1526A
markedly reduced ability to complement the cell lysis phenotype and temperature sensitivity of the Schizosaccharomyces pombe ags1-1 mutant, no accumulation of alpha-1,4-glucan
E1534A
able to complement the cell lysis phenotype and temperature sensitivity of the Schizosaccharomyces pombe ags1-1 mutant
G1165A
able to complement the cell lysis phenotype and temperature sensitivity of the Schizosaccharomyces pombe ags1-1 mutant
G696S
temperature-sensitive mutation, gene is functional at 28°C but not at 36°C
K1163Q
able to complement the cell lysis phenotype and temperature sensitivity of the Schizosaccharomyces pombe ags1-1 mutant
K1422Q
reduced accumulation of alpha-1,4-glucan
top
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.B3)
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)