Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.1.79 - maltose O-acetyltransferase and Organism(s) Bacillus subtilis and UniProt Accession P37515

for references in articles please use BRENDA:EC2.3.1.79
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.79 maltose O-acetyltransferase
IUBMB Comments
Not identical with EC 2.3.1.18, galactoside O-acetyltransferase. The acetyl group is added exclusively to the C6 position of glucose and to the C6 position of the non-reducing glucose residue of maltose . Other substrates of this enzyme are glucose, which is a better substrate than maltose , and mannose and frucose, which are poorer substrates than maltose . Isopropyl-beta-thio-galactose, which is a good substrate for EC 2.3.1.118 is a poor substrate for this enzyme .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Bacillus subtilis
UNIPROT: P37515
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
maltose o-acetyltransferase, maltose transacetylase, maa gene product, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
maltose transacetylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:maltose O-acetyltransferase
Not identical with EC 2.3.1.18, galactoside O-acetyltransferase. The acetyl group is added exclusively to the C6 position of glucose and to the C6 position of the non-reducing glucose residue of maltose [3]. Other substrates of this enzyme are glucose, which is a better substrate than maltose [2], and mannose and frucose, which are poorer substrates than maltose [2]. Isopropyl-beta-thio-galactose, which is a good substrate for EC 2.3.1.118 is a poor substrate for this enzyme [3].
CAS REGISTRY NUMBER
COMMENTARY hide
81295-47-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + maltose
CoA + 6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-D-glucose
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + maltose
CoA + 6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-D-glucose
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lo Leggio, L.; Dal Degan, F.; Poulsen, P.; Moeller Andersen, S.; Larsen, S.
The structure and specificity of Escherichia coli maltose acetyltransferase give new insight into the LacA family of acyltransferases
Biochemistry
42
5225-5235
2003
Bacillus subtilis (P37515), Escherichia coli (P77791), Escherichia coli
Manually annotated by BRENDA team