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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.49 - alpha-N-acetylgalactosaminidase and Organism(s) Elizabethkingia meningoseptica and UniProt Accession A4Q8F7

for references in articles please use BRENDA:EC3.2.1.49
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The human lysosomal enzyme is involved in the degradation of blood type A epitope.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Elizabethkingia meningoseptica
UNIPROT: A4Q8F7
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Elizabethkingia meningoseptica
The enzyme appears in selected viruses and cellular organisms
Synonyms
alpha-n-acetylgalactosaminidase, alpha-galnac, nagalase, envelope glycoprotein gp160, alpha-naga, alpha-galactosidase b, alpha-nagalase, alpha-galnacase i, alpha-nagal, alpha-galnacase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-acetamido-2-deoxy-alpha-D-galactoside acetamidodeoxygalactohydrolase
-
-
-
-
4-nitrophenyl-alpha-N-acetylgalactosaminidase
-
-
-
-
alpha-acetylgalactosaminidase
-
-
-
-
alpha-galactosidase B
-
-
-
-
alpha-N acetylgalactosaminidase
-
-
exo-alpha-N-acetylgalactosaminidase
-
-
-
-
N-acetyl-alpha-D-galactosaminidase
-
-
-
-
N-acetyl-alpha-galactosaminidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids
show the reaction diagram
a hydride at C3, activated by the interaction of the OH-3 hydroxyl with the conserved His228, is abstracted by NAD+ with oxidation of the OH-3 hydroxyl to a ketone. This activates H2 for proton abstraction by Tyr179, accompanied by elimination of the aglycone, thereby generating a 1,2-unsaturated intermediate. Water is then added to the anomeric center, followed by the reduction of the C3 ketone by the on-board NADH, completing the catalytic sequence and restoring NADH to NAD+ and the enzyme to its starting state to bind another substrate
Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids
show the reaction diagram
E2 elimination following hydride transfer from C3
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase
The human lysosomal enzyme is involved in the degradation of blood type A epitope.
CAS REGISTRY NUMBER
COMMENTARY hide
9075-63-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-nitrophenyl-alpha-N-acetylgalactosaminide + H2O
2-nitrophenol + alpha-N-acetylgalactosamine
show the reaction diagram
-
-
-
?
4-nitrophenyl 2-acetamido-2-deoxy-alpha-D-galactopyranoside + H2O
4-nitrophenol + 2-acetamido-2-deoxy-alpha-D-galactopyranose
show the reaction diagram
-
-
-
?
4-nitrophenyl N-acetyl-alpha-D-galactosamine + H2O
4-nitrophenol + N-acetyl-alpha-galactosamine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl N-acetyl-beta-D-galactosamine + H2O
4-nitrophenol + N-acetyl-beta-galactosamine
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
binds 1 NAD+ per subunit. The NAD+ cannot dissociate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19.7
4-nitrophenyl N-acetyl-alpha-D-galactosamine
-
recombinant enzyme, pH 7.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1250
4-nitrophenyl N-acetyl-alpha-D-galactosamine
-
recombinant enzyme, pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to the glycoside hydrolase family GH 109
additional information
-
comparison of the binding ability of alpha-N-acetylgalactosaminidase with red blood cells in different reaction buffers, such as normal saline, phosphate-buffered saline, a disodium hydrogen phosphate-based buffer, and 5% commercial glucose solution. Glucose buffer is suitable for blood group conversion with alpha-N acetylgalactosaminidase
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GH109_ELIME
444
0
50211
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 48500, SDS-PAGE
monomer
1 * 48500, SDS-PAGE
additional information
enzyme may exist both in the monomeric and dimeric form, depending on the salt concentration of the buffer solution
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme and in complex with alpha-N-acetylgalactosamine, to 2.3 and 2.4 A resolution, respectively. Each monomer of NagA consists of two closely associated domains, forming a narrow tunnel in which the NAD+ molecule is anchored. The NAD+ is embedded within a narrow tunnel, almost exclusively shielded from solvent. It is bound with its diphosphate group oriented towards the N-terminus of the first alpha-helix of the N-terminal dinucleotide-binding domain and has both the adenine ring and the nicotinamide ring in the anti conformation. No major structural changes are observed in NagA upon product binding
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
expression in Escherichia coli
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
alpha-N-acetylgalactosaminidase is an efficient enzyme for production of universal O blood cells
diagnostics
-
the enzyme is used for blood group conversion together with alpha-galactosidase, best in glucose buffer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sulzenbacher, G.; Liu, Q.; Bennett, E.; Levery, S.; Bourne, Y.; Ponchel, G.; Clausen, H.; Henrissat, B.
A novel alpha-N-acetylgalactosaminidase family with an NAD+-dependent catalytic mechanism suitable for enzymatic removal of blood group A antigens
Biocatal. Biotransform.
28
22-32
2010
Elizabethkingia meningoseptica (A4Q8F7)
-
Manually annotated by BRENDA team
Gao, H.; Li, S.; Bao, G.; Zhang, X.; Li, H.; Wang, Y.; Tan, Y.; Ji, S.; Gong, F.
Glucose buffer is suitable for blood group conversion with alpha-N acetylgalactosaminidase and alpha-galactosidase
Blood Transfus.
12
61-66
2014
Elizabethkingia meningoseptica
Manually annotated by BRENDA team
Chakladar, S.; Shamsi Kazem Abadi, S.; Bennet, A.
A mechanistic study on the alpha-N-acetylgalactosaminidase from E. meningosepticum: A family 109 glycoside hydrolase
MedChemComm
5
1188-1192
2014
Elizabethkingia meningoseptica
-
Manually annotated by BRENDA team
Molafilabi, A.; Shahabi, M.; Rafatpanah, H.; Mashkani, B.
Production of universal group O red blood cells by alpha-N-acetylgalactosaminidase enzyme expressed in Pichia pastoris
Indian J. Hematol. Blood Transfus.
35
125-130
2019
Elizabethkingia meningoseptica (A4Q8F7)
Manually annotated by BRENDA team