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Information on EC 3.1.3.8 - 3-phytase and Organism(s) Aspergillus awamori and UniProt Accession P34753

for references in articles please use BRENDA:EC3.1.3.8
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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.8 3-phytase
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This record set is specific for:
Aspergillus awamori
UNIPROT: P34753 not found.
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Word Map
The taxonomic range for the selected organisms is: Aspergillus awamori
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
microbial phytase, natuphos, alkaline phytase, 3-phytase, phytase a, beta-propeller phytase, atpap15, cell-bound phytase, appa2, acid phytase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-phytase
-
-
-
-
MYO-inositol-hexaphosphate 3-phosphohydrolase
-
-
-
-
pGF11 phytase
-
recombinant enzyme
pGP209 phytase
-
recombinant enzyme
pH 2.5 optimum acid phosphatase
-
-
-
-
phytase
-
-
-
-
phytate 1-phosphatase
-
-
-
-
Phytate 3-phosphatase
-
-
-
-
phytate 6-phosphatase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
myo-inositol-hexakisphosphate 3-phosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37288-11-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
myo-inositol hexakisphosphate + H2O
? + phosphate
show the reaction diagram
constitutive enzyme
-
?
myo-inositol hexakisphosphate + H2O
1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
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
myo-inositol hexakisphosphate + H2O
? + phosphate
show the reaction diagram
constitutive enzyme
-
?
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
recombinant enzyme pGP209
60
-
wild type PhyA
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
var. awamorii ATCC 38854. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHYA_ASPAW
467
0
51075
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
-
SDS-PAGE, wild type enzyme PyhA
84000
-
SDS-PAGE, recombinant enzyme pGP209
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 70
-
the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation, the activity is negligible at 70°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Sephadex G-100 gel filtration and DEAE-Sepharose CL-6B anion exchange column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Aspergillus awamori strains pGP209 and pGF11
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the enzyme denatures at temperatures of 50°C or above, when the temperature is reduced again the protein refolds almost entirely into a fully active, native conformation
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shieh, T.R.; Ware, J.H.
Survey of microorganisms for the production of extracellular phytase
Appl. Microbiol.
16
1348-1351
1968
Aspergillus awamori, Aspergillus carbonarius, Aspergillus ficuum, Aspergillus ficuum K, Aspergillus ficuum NRRL 3135, Aspergillus ficuum WB 320, Aspergillus ficuum WB 364, Aspergillus ficuum WB 4016, Aspergillus ficuum WB 4541, Aspergillus ficuum WB4781, Aspergillus ficuum X, Aspergillus flavus, Aspergillus niger, Aspergillus niger NRRL 326, Aspergillus niger NRRL 330, Aspergillus niger NRRL 372, Aspergillus niger NRRL 4361, Aspergillus niger NRRL337, Aspergillus niger NRRL372, Aspergillus phoenicis, Aspergillus terreus, Aspergillus tubingensis, Aspergillus tubingensis NRRL 4875, Aspergillus versicolor
Manually annotated by BRENDA team
Vohra, A.; Satyanarayana, T.
Phytases: microbial sources, production, purification, and potential biotechnological applications
Crit. Rev. Biotechnol.
23
29-60
2003
Aspergillus amstelodami, Aspergillus awamori (P34753), Aspergillus candidus, Aspergillus carbonarius, Aspergillus carneus, Aspergillus chevalieri, Aspergillus flavus, Aspergillus fumigatus (O00092), Aspergillus nidulans, Aspergillus nidulans (O00093), Aspergillus niger (O93838), Aspergillus niger (P34752), Aspergillus niger SK57 (O93838), Aspergillus pseudoglaucus, Aspergillus syndowi, Aspergillus terreus (O00085), Aspergillus terreus CBS (O00085), Aspergillus versicolor, Aspergillus wentii, Bacillus amyloliquefaciens, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) DS1, Bacillus subtilis, Blastobotrys adeninivorans, Botrytis cinerea, Candida tropicalis, Clavispora lusitaniae, Cyberlindnera rhodanensis, Enterobacter sp., Escherichia coli, Geotrichum candidum, Hanseniaspora valbyensis, Klebsiella aerogenes, Klebsiella oxytoca, Kluyveromyces lactis, Lachancea kluyveri, Lachancea thermotolerans, Lactobacillus amylovorus, Metschnikowia pulcherrima, Mitsuokella multacida, Mucor piriformis, Mucor racemosus, Neurospora sp., Penicillium caseoicolum, Penicillium sp., Pseudomonas sp., Rhizopus arrhizus, Rhizopus microsporus var. oligosporus, Rhizopus stolonifer, Scheffersomyces spartinae, Schwanniomyces castellii, Schwanniomyces occidentalis, Schwanniomyces yamadae, Selenomonas ruminantium, Thermomyces dupontii (O00096), Thermomyces lanuginosus, Thermothelomyces heterothallicus, Thermothelomyces heterothallicus (O00107), Torulaspora delbrueckii, Torulaspora globosa, Torulaspora pretoriensis, Wickerhamomyces anomalus, [Candida] intermedia
Manually annotated by BRENDA team
Martin, J.A.; Murphy, R.A.; Power, R.F.
Purification and physico-chemical characterisation of genetically modified phytases expressed in Aspergillus awamori
Biores. Technol.
97
1703-1708
2006
Aspergillus awamori, Aspergillus niger, Aspergillus sp.
Manually annotated by BRENDA team