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Information on EC 3.2.1.22 - alpha-galactosidase and Organism(s) Rhizopus sp. ACCC 30795 and UniProt Accession C7SEV1

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IUBMB Comments
Also hydrolyses alpha-D-fucosides.
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This record set is specific for:
Rhizopus sp. ACCC 30795
UNIPROT: C7SEV1
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The taxonomic range for the selected organisms is: Rhizopus sp. ACCC 30795
The enzyme appears in selected viruses and cellular organisms
Synonyms
alpha-galactosidase, alpha-galactosidase a, alpha-gal, alpha-gal a, agalsidase alfa, genzyme, alpha-d-galactosidase, a-galactosidase, fabrazyme, alpha-galactosidase i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Agalsidase alfa
-
-
-
-
alpha-D-galactosidase
-
-
-
-
Alpha-D-galactoside galactohydrolase
-
-
-
-
alpha-galactosidase A
-
-
-
-
alpha-galactoside galactohydrolase
-
-
-
-
ceramidase, galactosylgalactosylglucosyl-
-
-
-
-
ceramide trihexosidase
-
-
-
-
ceramidetrihexosidase
-
-
-
-
ceramidetrihexoside-alpha-galactosidase
-
-
-
-
melibiase
-
-
-
-
trihexosyl ceramide galactosidase
-
-
-
-
trihexosylceramide alpha-galactosidase
-
-
-
-
trihexosylceramidealpha-galactosidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-galactoside galactohydrolase
Also hydrolyses alpha-D-fucosides.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-01-2
-
9025-35-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-D-galactoside + H2O
4-nitrophenol + alpha-D-galactose
show the reaction diagram
-
-
-
?
melibiose + H2O
D-galactose + D-glucose
show the reaction diagram
-
-
-
?
raffinose + H2O
sucrose + alpha-D-galactose
show the reaction diagram
-
-
-
?
stachyose + 2 H2O
2 alpha-D-galactose + sucrose
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cr3+
the activity of recombinant Aga-F78 is significantly enhanced in the presence of Cr3+
Fe3+
the activity of recombinant Aga-F78 is significantly enhanced in the presence of Fe3+
Pb2+
the activity of recombinant Aga-F78 is significantly enhanced in the presence of Pb2+
additional information
the addition of other metal ions or chemicals has little or no effect on the activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
strong inhibitor
Hg2+
strong inhibitor
Mn2+
strong inhibitor
SDS
strong inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
the activity of recombinant Aga-F78 is significantly enhanced in the presence of EDTA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56.61
after 2461.3fold purification, using 4-nitrophenyl alpha-D-galactoside as substrate, at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
C7SEV1_9FUNG
724
0
82007
TrEMBL
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
210000
gel filtration
82000
3 * 82000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
3 * 82000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
highly pH stable over the pH range 5.0-10.0
705088
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 60
the recombinant enzyme loses about 60% of the initial activity after incubation at 50°C for 30 min and is completely inactivated at 60°C for 5 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is protease-resistant, when combined with trypsin, the enzyme retained over 90% degradability to soybean meal
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cao, Y.; Wang, Y.; Luo, H.; Shi, P.; Meng, K.; Zhou, Z.; Zhang, Z.; Yao, B.
Molecular cloning and expression of a novel protease-resistant GH-36 alpha-galactosidase from Rhizopus sp. F78 ACCC 30795
J. Microbiol. Biotechnol.
19
1295-1300
2009
Rhizopus sp. ACCC 30795 (C7SEV1)
Manually annotated by BRENDA team