About: Aspergillus oryzae alpha-amylase

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About: Aspergillus oryzae alpha-amylase Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

fungal protein found in Aspergillus oryzae RIB40

Attributes	Values
rdf:type	Item
description	білок грибів, наявний в Aspergillus oryzae RIB40 (uk) fungal protein found in Aspergillus oryzae RIB40 (en) proteïne in AO090023000944-T (nl)
rdfs:label	AO090023000944-T (nl) Aspergillus oryzae alpha-amylase (en)
skos:prefLabel	AO090023000944-T (nl) Aspergillus oryzae alpha-amylase (en)
name	AO090023000944-T (nl) Aspergillus oryzae alpha-amylase (en)
instance of	wds:Q62784837-DE062432-64BA-4EE8-B2D6-12D8BA42D9ED
part of	wds:Q62784837-ccdbfae8-42c6-4aca-f5a2-14fa250489a2
instance of	protein
part of	Alpha amylase, subgroup
has use	wds:Q62784837-2ED1B052-5351-4A84-A52E-E165D64BCF60
has use	food additive
found in taxon	wds:Q62784837-7936443D-D220-48C0-AE23-8D38FFFA958A
found in taxon	Aspergillus oryzae RIB40
GeneDB ID	wds:Q62784837-D44B2A82-0D90-400E-A50E-41447233F83B
GeneDB ID	AO090023000944-T
skos:altLabel	Alpha-amylase (en)
encoded by	wds:Q62784837-9406A936-765D-43D0-9AC3-6956E14FC1B6
encoded by	amyC
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q62784837
is main subject of	Functional elements of the promoter region of the Aspergillus oryzae glaA gene encoding glucoamylase Construction of a fusion gene comprising the Taka-amylase A promoter and the Escherichia coli beta-glucuronidase gene and analysis of its expression in Aspergillus oryzae. Septum-directed secretion in the filamentous fungus Aspergillus oryzae. In vivo imaging of endoplasmic reticulum and distribution of mutant α-amylase in Aspergillus oryzae Structure and molecular model refinement of Aspergillus oryzae (TAKA) alpha-amylase: an application of the simulated-annealing method Autophagy delivers misfolded secretory proteins accumulated in endoplasmic reticulum to vacuoles in the filamentous fungus Aspergillus oryzae. Physiological characterisation of recombinant Aspergillus nidulans strains with different creA genotypes expressing A. oryzae alpha-amylase The enzymatic and molecular characteristics of Saccharomycopsis alpha-amylase secreted from Saccharomyces cerevisiae Proteomic analysis of extracellular proteins from Aspergillus oryzae grown under submerged and solid-state culture conditions Loss of Aspergillus oryzae amyR function indirectly affects hemicellulolytic and cellulolytic enzyme production Improvement of heterologous protein production in Aspergillus oryzae by RNA interference with alpha-amylase genes. Analysis of secreted proteins during conidial germination of Aspergillus oryzae RIB40. Insertion analysis of putative functional elements in the promoter region of the Aspergillus oryzae Taka-amylase A gene (amyB) using a heterologous Aspergillus nidulans amdS-lacZ fusion gene system Taka-amylase A in the conidia of Aspergillus oryzae RIB40. Specific expression and temperature-dependent expression of the acid protease-encoding gene (pepA) in Aspergillus oryzae in solid-state culture (Rice-Koji) Some distinguishable properties between acid-stable and neutral types of alpha-amylases from acid-producing koji A comparison of the unfolded protein response in solid-state with submerged cultures of Aspergillus oryzae. Analysis of extracellular proteins of Aspergillus oryzae grown on soy sauce koji Improvement of promoter activity by the introduction of multiple copies of the conserved region III sequence, involved in the efficient expression of Aspergillus oryzae amylase-encoding genes Nonfunctionality of Aspergillus sojae aflR in a strain of Aspergillus parasiticus with a disrupted aflR gene. Deletion analysis of the Taka-amylase A gene promoter using a homologous transformation system in Aspergillus oryzae Isolation of a cDNA encoding Aspergillus oryzae Taka-amylase A: evidence for multiple related genes Aspergillus nidulans nuclear proteins bind to a CCAAT element and the adjacent upstream sequence in the promoter region of the starch-inducible Taka-amylase A gene Studies on the active site of Taka-amylase A: its action on phenyl maltooligosides with a charge at their non-reducing-ends An overview of the CCAAT-box binding factor in filamentous fungi: assembly, nuclear translocation, and transcriptional enhancement. Kinetic Study on Chemical Modification of Taka-Amylase A. II. Ethoxycarbonylation of Histidine Residues Studies on the substrate specificity of Taka-amylase A. XII. Investigation of the active site of Taka-amylase A by examining the properties of p-phenylazobenzoyl Taka-amylase A Sequence-specific binding sites in the Taka-amylase A G2 promoter for the CreA repressor mediating carbon catabolite repression. [Regulation of gene expression in Aspergilli] Production of a fungal protein, Taka-amylase A, by protein-producing Bacillus brevis HPD31 Structural consequences of neopullulanase mutations Contribution ratios of amyA, amyB, amyC genes to high-level α-amylase expression in Aspergillus oryzae Identification of potential cell wall component that allows Taka-amylase A adsorption in submerged cultures of Aspergillus oryzae Chaperonin GroE-facilitated refolding of disulfide-bonded and reduced Taka-amylase A from Aspergillus oryzae Molecular breeding of yeast with higher metal-adsorption capacity by expression of histidine-repeat insertion in the protein anchored to the cell wall Characteristic expression of three amylase-encoding genes, agdA, amyB, and glaA in Aspergillus oryzae transformants containing multiple copies of the agdA gene Modification of subsite Lys residue induced a large increase in maltosidase activity of Taka-amylase A
is main subject of	wds:Q41727542-C7AE7E70-1BEF-43FD-932D-95AFF673DAFE wds:Q54317813-E290FA98-C9AC-42A0-A70A-2EFAD8E1B553 wds:Q62784852-B87C411B-D846-4E8F-8F7C-0A62EB8A4BC0 wds:Q36321677-8558722B-FED4-49B9-882B-9FB724CE80F6 wds:Q38348595-B40BF661-0092-402D-9F37-2884FA4884C0 wds:Q33242151-CBDB5596-2DE2-4526-A50F-8C6ACF79C129 wds:Q46269680-5D542770-914D-4F9F-8CB9-697C32F44ED2 wds:Q50526450-3154AE14-A167-484A-91E9-28561CD3C33E wds:Q62776118-05028F42-308C-4A6A-92A2-892690DC0461 wds:Q62784856-9CF08A44-8ADE-43DF-82B2-24F708ADCED6 wds:Q28341351-396FE22C-C52E-4DB3-8EDB-4CA181B542E5 wds:Q33398314-94842427-7413-464F-B8CC-6794FCD633FA wds:Q57753381-FCD6B25D-890E-45B3-98F0-13F934F8B6EC wds:Q62653121-7E4F6277-779D-4853-AFEE-C28F0E227595 wds:Q54690686-D7829D95-6D99-45FF-AC19-966B5B31586B wds:Q47244404-10CF362A-FB5F-4299-9887-B9C2B21B0461 wds:Q50520828-1A9680C4-37A7-4E24-82B2-B83F818B38C9 wds:Q57663731-E9446FAE-2AFB-405A-8778-855DA5334798 wds:Q62784842-FBF7F21E-38A4-4F4A-9641-D50C6E46C096 wds:Q62784846-1FCAE222-89F1-4C2F-813A-67B6D6648121 wds:Q35679086-B2A4DF52-0D26-444D-BB25-A867C9CA0115 wds:Q42477780-6E60E783-B6F1-41D9-805C-FD349D3FCDFE wds:Q54577600-5E975C77-7D26-4763-B894-32971A28DB7E wds:Q36105336-FA478C65-316B-4C8F-81D5-73DEFB8763E6 wds:Q45201022-0EA98808-7315-4C4F-B7B5-42A2B4BEE49D wds:Q62647684-FD0AF96F-21C4-4294-AD51-852B2EAEC89A wds:Q62776120-5A1A48A1-DA10-4A6A-9E36-F4C1AEF6FC3E wds:Q62784844-FE92EB57-A0A7-4C54-867D-CDEF5AAB0316 wds:Q27654255-DB62A210-38F0-41DB-B94E-7837FB43A44F wds:Q37034671-FBF2FDDD-A41C-4687-9D4F-A0661FE01938 wds:Q39640303-204F4D98-3989-4B0E-B594-0260DC2B24EE wds:Q46041508-B5CC117B-09E4-437C-9ED4-98E687C19E03 wds:Q43786606-DC552213-42C9-4238-B234-82BAC05175FA wds:Q62784854-DF791E68-66C2-465E-97C6-1D17820CE232 wds:Q62751110-F9195DA7-D992-466F-92CD-039ED2BB6970 wds:Q62784848-6EF7D184-D6C0-4FE9-B3D0-B41015B471D9 wds:Q62784850-DDCD199C-DF1B-4ACB-8FDD-75D32D5C1A16
is encodes of	amyC
is encodes of	wds:Q62784857-9ADC67E5-B9E6-4A50-B940-937FA6CBCD22

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