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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.3.26 - 4-phytase and Organism(s) Aspergillus terreus and UniProt Accession O00085

for references in articles please use BRENDA:EC3.1.3.26
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.26 4-phytase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Aspergillus terreus
UNIPROT: O00085 not found.
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: Aspergillus terreus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
phytase, purple acid phosphatase, 6-phytase, histidine acid phosphatase, ronozyme, phytase b, phya2, multiple inositol polyphosphate phosphatase, phya1, minpp, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-phytase
-
-
-
-
phytase
-
-
-
-
phytate 6-phosphatase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
myo-inositol-hexakisphosphate 4-phosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9001-89-2
-
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
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHYA1_ASPTE
466
0
51093
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A68S/A72E/A73E/S77N
-
t1/2 at 49°C decreases from 53 min for the wild-type enzyme to 20 min for the mutant enzyme
E41A/D42G
-
t1/2 at 49°C increases from 53 min for the wild-type enzyme to 76 min for the mutant enzyme
H61E
-
t1/2 at 49°C increases from 53 min for the wild-type enzyme to 54 min for the mutant enzyme
additional information
-
replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49
-
t1/2: 53 min, wild-type enzyme
additional information
-
replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of mutant enzymes in Aspergillus niger
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
about two-third of phosphorus of feedstuffs of plant origin is present as phytic acid in form of phytate. Under most dietary conditions, phytate phosphate is unavailable to poultry. Addition of phytase to feed can fully replace phosphorus supplementation. Phytase can increase the use of low-cost plant meals in the aquaculture industry and maintains acceptable phosphorus levels in the water
synthesis
preparation of myo-inositol phosphates as tools for metabolic investigation, enzyme stabilizers, as enzyme inhibitors and therefore potential drugs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Jermutus, L.; Tessier, M.; Pasamontes, L.; van Loon, A.P.; Lehmann, M.
Structure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case
J. Biotechnol.
85
15-24
2001
Aspergillus niger, Aspergillus terreus, Aspergillus terreus 9A-1
Manually annotated by BRENDA team