SK284945B6 - DNA kódujúca chinoloxidázu cytochrómu typu bd z Brevibacterium lactofermentum - Google Patents
DNA kódujúca chinoloxidázu cytochrómu typu bd z Brevibacterium lactofermentum Download PDFInfo
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- SK284945B6 SK284945B6 SK771-99A SK77199A SK284945B6 SK 284945 B6 SK284945 B6 SK 284945B6 SK 77199 A SK77199 A SK 77199A SK 284945 B6 SK284945 B6 SK 284945B6
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- amino acid
- cyda
- seq
- cytochrome
- quinoloxidase
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- ZSXJENBJGRHKIG-UWVGGRQHSA-N Tyr-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 ZSXJENBJGRHKIG-UWVGGRQHSA-N 0.000 description 1
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- ISERLACIZUGCDX-ZKWXMUAHSA-N Val-Asp-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](C(C)C)N ISERLACIZUGCDX-ZKWXMUAHSA-N 0.000 description 1
- SCBITHMBEJNRHC-LSJOCFKGSA-N Val-Asp-Val Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](C(C)C)C(=O)O)N SCBITHMBEJNRHC-LSJOCFKGSA-N 0.000 description 1
- TVGWMCTYUFBXAP-QTKMDUPCSA-N Val-Thr-His Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)NC(=O)[C@H](C(C)C)N)O TVGWMCTYUFBXAP-QTKMDUPCSA-N 0.000 description 1
- ZLMFVXMJFIWIRE-FHWLQOOXSA-N Val-Trp-Leu Chemical compound CC(C)C[C@@H](C(=O)O)NC(=O)[C@H](CC1=CNC2=CC=CC=C21)NC(=O)[C@H](C(C)C)N ZLMFVXMJFIWIRE-FHWLQOOXSA-N 0.000 description 1
- 238000000862 absorption spectrum Methods 0.000 description 1
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- 239000011543 agarose gel Substances 0.000 description 1
- 108010070944 alanylhistidine Proteins 0.000 description 1
- 108010011559 alanylphenylalanine Proteins 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- KOSRFJWDECSPRO-UHFFFAOYSA-N alpha-L-glutamyl-L-glutamic acid Natural products OC(=O)CCC(N)C(=O)NC(CCC(O)=O)C(O)=O KOSRFJWDECSPRO-UHFFFAOYSA-N 0.000 description 1
- 238000003277 amino acid sequence analysis Methods 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 108010077245 asparaginyl-proline Proteins 0.000 description 1
- 108010069205 aspartyl-phenylalanine Proteins 0.000 description 1
- 230000002715 bioenergetic effect Effects 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- BHQCQFFYRZLCQQ-OELDTZBJSA-N cholic acid Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 BHQCQFFYRZLCQQ-OELDTZBJSA-N 0.000 description 1
- 229960002471 cholic acid Drugs 0.000 description 1
- 235000019416 cholic acid Nutrition 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 108010004073 cysteinylcysteine Proteins 0.000 description 1
- 108010060199 cysteinylproline Proteins 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 229960003964 deoxycholic acid Drugs 0.000 description 1
- KXGVEGMKQFWNSR-UHFFFAOYSA-N deoxycholic acid Natural products C1CC2CC(O)CCC2(C)C2C1C1CCC(C(CCC(O)=O)C)C1(C)C(O)C2 KXGVEGMKQFWNSR-UHFFFAOYSA-N 0.000 description 1
- 230000003467 diminishing effect Effects 0.000 description 1
- 108010054813 diprotin B Proteins 0.000 description 1
- 230000037149 energy metabolism Effects 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 108010055341 glutamyl-glutamic acid Proteins 0.000 description 1
- 108010079547 glutamylmethionine Proteins 0.000 description 1
- KZNQNBZMBZJQJO-YFKPBYRVSA-N glyclproline Chemical compound NCC(=O)N1CCC[C@H]1C(O)=O KZNQNBZMBZJQJO-YFKPBYRVSA-N 0.000 description 1
- 108010089804 glycyl-threonine Proteins 0.000 description 1
- 108010077515 glycylproline Proteins 0.000 description 1
- 108010036413 histidylglycine Proteins 0.000 description 1
- 108010025306 histidylleucine Proteins 0.000 description 1
- 108010018006 histidylserine Proteins 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 108010076756 leucyl-alanyl-phenylalanine Proteins 0.000 description 1
- 108010044056 leucyl-phenylalanine Proteins 0.000 description 1
- 108010030617 leucyl-phenylalanyl-valine Proteins 0.000 description 1
- 108010091871 leucylmethionine Proteins 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 108010003700 lysyl aspartic acid Proteins 0.000 description 1
- 108010025153 lysyl-alanyl-alanine Proteins 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 108010073440 menaquinol oxidase Proteins 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 108010005942 methionylglycine Proteins 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- IRTNBRZQXRDXSN-UHFFFAOYSA-N n-methyl-n-(1-nitro-6-oxo-7h-purin-2-yl)nitrous amide Chemical compound O=C1N([N+]([O-])=O)C(N(N=O)C)=NC2=C1NC=N2 IRTNBRZQXRDXSN-UHFFFAOYSA-N 0.000 description 1
- UMWKZHPREXJQGR-XOSAIJSUSA-N n-methyl-n-[(2s,3r,4r,5r)-2,3,4,5,6-pentahydroxyhexyl]decanamide Chemical compound CCCCCCCCCC(=O)N(C)C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO UMWKZHPREXJQGR-XOSAIJSUSA-N 0.000 description 1
- 230000036284 oxygen consumption Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
- 108010084525 phenylalanyl-phenylalanyl-glycine Proteins 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- NRHMKIHPTBHXPF-TUJRSCDTSA-M sodium cholate Chemical compound [Na+].C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC([O-])=O)C)[C@@]2(C)[C@@H](O)C1 NRHMKIHPTBHXPF-TUJRSCDTSA-M 0.000 description 1
- FHHPUSMSKHSNKW-SMOYURAASA-M sodium deoxycholate Chemical compound [Na+].C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC([O-])=O)C)[C@@]2(C)[C@@H](O)C1 FHHPUSMSKHSNKW-SMOYURAASA-M 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- 230000004102 tricarboxylic acid cycle Effects 0.000 description 1
- 108010080629 tryptophan-leucine Proteins 0.000 description 1
- 108010038745 tryptophylglycine Proteins 0.000 description 1
- 108010044292 tryptophyltyrosine Proteins 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0012—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7)
- C12N9/0036—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on NADH or NADPH (1.6)
- C12N9/0038—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on NADH or NADPH (1.6) with a heme protein as acceptor (1.6.2)
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Physics & Mathematics (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP10164019A JPH11346776A (ja) | 1998-06-11 | 1998-06-11 | ブレビバクテリウム・ラクトファーメンタムのシトクロムbd型キノールオキシダーゼ遺伝子 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| SK77199A3 SK77199A3 (en) | 2000-05-16 |
| SK284945B6 true SK284945B6 (sk) | 2006-03-02 |
Family
ID=15785252
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SK771-99A SK284945B6 (sk) | 1998-06-11 | 1999-06-09 | DNA kódujúca chinoloxidázu cytochrómu typu bd z Brevibacterium lactofermentum |
Country Status (13)
| Country | Link |
|---|---|
| US (1) | US6156886A (es) |
| EP (1) | EP0967282B1 (es) |
| JP (1) | JPH11346776A (es) |
| KR (1) | KR100629091B1 (es) |
| CN (1) | CN1160459C (es) |
| AU (1) | AU749069B2 (es) |
| BR (1) | BR9902248A (es) |
| DE (1) | DE69926691T2 (es) |
| ID (1) | ID22875A (es) |
| MY (1) | MY114645A (es) |
| PE (1) | PE20000759A1 (es) |
| PL (1) | PL195017B1 (es) |
| SK (1) | SK284945B6 (es) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH11346776A (ja) * | 1998-06-11 | 1999-12-21 | Ajinomoto Co Inc | ブレビバクテリウム・ラクトファーメンタムのシトクロムbd型キノールオキシダーゼ遺伝子 |
| JP4380029B2 (ja) | 2000-07-05 | 2009-12-09 | 味の素株式会社 | 微生物を利用した物質の製造法 |
| JP2002078490A (ja) * | 2000-09-06 | 2002-03-19 | Ajinomoto Co Inc | コリネ型細菌の呼吸鎖酵素遺伝子 |
| US20040014180A1 (en) * | 2000-09-14 | 2004-01-22 | Michael Bott | Method for the microbial production of metabolic products, polynucleotides from coryneform bacteria and use thereof |
| CN100475960C (zh) * | 2002-02-26 | 2009-04-08 | 纳幕尔杜邦公司 | 遗传元件的重组方法 |
| US6977162B2 (en) * | 2002-03-01 | 2005-12-20 | Ravgen, Inc. | Rapid analysis of variations in a genome |
| US7727720B2 (en) | 2002-05-08 | 2010-06-01 | Ravgen, Inc. | Methods for detection of genetic disorders |
| US7442506B2 (en) | 2002-05-08 | 2008-10-28 | Ravgen, Inc. | Methods for detection of genetic disorders |
| US7026233B2 (en) * | 2003-08-06 | 2006-04-11 | Taiwan Semiconductor Manufacturing Company, Ltd. | Method for reducing defects in post passivation interconnect process |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TW256842B (es) * | 1991-12-17 | 1995-09-11 | Takeda Pharm Industry Co Ltd | |
| TW293827B (es) * | 1992-04-20 | 1996-12-21 | Takeda Pharm Industry Co Ltd | |
| TW293022B (es) * | 1992-07-27 | 1996-12-11 | Takeda Pharm Industry Co Ltd | |
| DE4411864A1 (de) * | 1994-04-08 | 1995-10-12 | Basf Schwarzheide Gmbh | Verfahren zur Herstellung von harten bis zähharten Polyurethanschaumstoffen mit erhöhtem Anteil an offenen Zellen und vermindertem Schrumpf |
| DE4418507A1 (de) * | 1994-05-27 | 1995-11-30 | Bayer Ag | Verfahren zur Herstellung offenzelliger Polyurethan-Hartschaumstoffe und ihre Verwendung als Isoliermaterial in Paneelen und als Isolierschaumstoffe |
| DE19545165A1 (de) * | 1995-12-04 | 1997-06-05 | Basf Ag | Verfahren zur Herstellung von offenzelligen Polyurethan-Schaumstoffen |
| US5721284A (en) * | 1996-12-20 | 1998-02-24 | The Dow Chemical Company | Open-celled rigid polyurethane foam |
| DE19742013A1 (de) * | 1997-09-24 | 1999-03-25 | Basf Ag | Offenzellige Hartschaumstoffe auf Isocyanatbasis |
| JPH11346776A (ja) * | 1998-06-11 | 1999-12-21 | Ajinomoto Co Inc | ブレビバクテリウム・ラクトファーメンタムのシトクロムbd型キノールオキシダーゼ遺伝子 |
-
1998
- 1998-06-11 JP JP10164019A patent/JPH11346776A/ja active Pending
-
1999
- 1999-06-08 US US09/327,504 patent/US6156886A/en not_active Expired - Lifetime
- 1999-06-08 AU AU33926/99A patent/AU749069B2/en not_active Ceased
- 1999-06-09 MY MYPI99002360A patent/MY114645A/en unknown
- 1999-06-09 SK SK771-99A patent/SK284945B6/sk unknown
- 1999-06-09 PE PE1999000515A patent/PE20000759A1/es not_active Application Discontinuation
- 1999-06-09 EP EP99110980A patent/EP0967282B1/en not_active Expired - Lifetime
- 1999-06-09 DE DE69926691T patent/DE69926691T2/de not_active Expired - Lifetime
- 1999-06-10 ID IDP990560A patent/ID22875A/id unknown
- 1999-06-11 KR KR1019990021716A patent/KR100629091B1/ko not_active Expired - Fee Related
- 1999-06-11 CN CNB991084500A patent/CN1160459C/zh not_active Expired - Fee Related
- 1999-06-11 BR BR9902248-6A patent/BR9902248A/pt not_active Application Discontinuation
- 1999-06-11 PL PL333692A patent/PL195017B1/pl unknown
Also Published As
| Publication number | Publication date |
|---|---|
| US6156886A (en) | 2000-12-05 |
| EP0967282A3 (en) | 2001-12-05 |
| KR20000006104A (ko) | 2000-01-25 |
| EP0967282A2 (en) | 1999-12-29 |
| SK77199A3 (en) | 2000-05-16 |
| AU749069B2 (en) | 2002-06-20 |
| BR9902248A (pt) | 2000-05-02 |
| KR100629091B1 (ko) | 2006-09-28 |
| JPH11346776A (ja) | 1999-12-21 |
| ID22875A (id) | 1999-12-16 |
| AU3392699A (en) | 1999-12-23 |
| DE69926691D1 (de) | 2005-09-22 |
| CN1239142A (zh) | 1999-12-22 |
| PL195017B1 (pl) | 2007-08-31 |
| PL333692A1 (en) | 1999-12-20 |
| CN1160459C (zh) | 2004-08-04 |
| MY114645A (en) | 2002-11-30 |
| EP0967282B1 (en) | 2005-08-17 |
| PE20000759A1 (es) | 2000-08-29 |
| DE69926691T2 (de) | 2006-06-14 |
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