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"sulfur oxygenase reductase"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
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  • ¿µ¹®
    ÇѱÛ
  • cyclo-oxygenase
    ½ÃŬ·Î¿Á½Ã°Ô³ª¾ÆÁ¦
  • aldehyde reductase
    ¾Ëµ¥È÷µåȯ¿øÈ¿¼Ò
  • reductase
    ȯ¿øÈ¿¼Ò
  • sublimed sulfur
    ½ÂȭȲ
  • sulfur
    Ȳ
  • sulfur bacterium
    À¯È²±Õ
  • sulfur dioxide
    ÀÌ»êȭȲ
  • sulfur granule
    À¯È²°ú¸³
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 3 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • sulfur granule
    À¯È²°ú¸³
  • sulfur dioxide
    ÀÌ»êȭȲ
  • sulfur
    Ȳ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 12 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • cyclo-oxygenase
    ½ÃŬ·Î¿Á½Ã°Ô³ª¾ÆÁ¦
  • reductase
    ȯ¿øÈ¿¼Ò
  • sulfur bacterium
    À¯È²±Õ
  • sulfur dioxide control
    ÀÌ»êȭȲ°¡½º±ÔÁ¦
  • sulfur granule
    À¯È²°ú¸³
  • hepatic sulfur
    °£È²
  • monoclinic sulfur
    ´Ü»çÁ¤°èȲ
  • roll sulfur
    ¸·´ëȲ
  • sulfur
    Ȳ
  • sulfur dioxide
    ÀÌ»êȭȲ
  • sublimed sulfur
    ½ÂȭȲ
  • washed sulfur
    Á¤¼¼È²
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 14 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • reductase, 5-alpha-reductase inhibitor
    5a-ȯ¿øÈ¿¼Ò¾ïÁ¦Á¦(¡­ü½êªý£áÈåäð¤ð¥),5a-¸®´öÅ×À̽º¾ïÁ¦Á¦(¡­åäð¤ð¥)
  • Cyclo-oxygenase
    »çÀÌŬ·Î¿Á½Ã°Ô³×ÀÌÁî
  • granule, sulfur(-phur)
    Ȳ»ö°ú¸³, À¯È²»ö°ú¸³
  • hepatic sulfur
    °£È²(ÊÜüÜ).
  • NADH-cytochrome b5 reductase
    NADH-½ÃÅäÅ©·Òb5¸®´öŸ¾ÆÁ¦
  • NADH-methemoglobin reductase
    NADH-¸ÞÆ®Çì¸ð±Û·Îºó ȯ¿øÈ¿¼Ò
  • NADPH-dependent methemoglobin reductase
    NADH-ÀÇÁ¸¸ÞÆ®Çì¸ð±Û·Îºó ¸®´öŸ¾ÆÁ¦
  • glutathione reductase
    ±Û·çŸƼ¿Â ¸®´ÚŸÁ¦<ȯ¿øÈ¿¼Ò>.
  • glutathione reductase
    ±Û·çŸƼ¿Â¸®´ÚŸÁ¦<--ȯ¿øÈ¿¼Ò>
  • glutathione reductase deficiency
    ±Û·çŸƼ¿Â ȯ¿øÈ¿¼Ò °áÇÌÁõ.
  • glyoxylate reductase
    ±Û¸®¿Á½Ç»êȯ¿øÈ¿¼Ò.
  • reductase
    ¸®´öŸ¾ÆÁ¦, ȯ¿øÈ¿¼Ò(ü½êªý£áÈ).
  • reductase
    ȯ¿øÈ¿¼Ò
  • reductase test
    ȯ¿øÈ¿¼Ò½ÃÇè.
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  • ¿µ¹®
    ÇѱÛ
  • reductase, 5-alpha-reductase inhibitor
    5a-ȯ¿øÈ¿¼Ò¾ïÁ¦Á¦(¡­ü½êªý£áÈåäð¤ð¥),5a-¸®´öÅ×À̽º¾ïÁ¦Á¦(¡­åäð¤ð¥)
  • oxygenase
    ¿Á½Ã°Ô³ªÁ¦.
  • cystine reductase
    ½Ã½ºÆ¾È¯¿øÈ¿¼Ò(¡­ü½êª ý£áÈ).
  • cytochrome b5 reductase deficiency
    ½ÃÅäÅ©·Ò b5 ȯ¿øÈ¿¼Ò °áÇÌ
  • cytochrome reductase
    ½ÃÅäÅ©·Ò ·¹´ÚŸÁ¦<ȯ¿øÈ¿¼Ò(ü½êªý£áÈ)>.
  • dihydropteridine reductase
    Dihydropteridine reductase
  • glutathione reductase
    ±Û·çŸƼ¿Â¸®´ÚŸÁ¦<--ȯ¿øÈ¿¼Ò>
  • glutathione reductase
    ±Û·çŸƼ¿Â ¸®´ÚŸÁ¦<ȯ¿øÈ¿¼Ò>.
  • glutathione reductase deficiency
    ±Û·çŸƼ¿Â ȯ¿øÈ¿¼Ò °áÇÌÁõ.
  • glyoxylate reductase
    ±Û¸®¿Á½Ç»êȯ¿øÈ¿¼Ò.
  • glyoxylic acid reductase deficency
  • reductase
    ȯ¿øÈ¿¼Ò
  • reductase
    ¸®´öŸ¾ÆÁ¦, ȯ¿øÈ¿¼Ò(ü½êªý£áÈ).
  • reductase test
    ȯ¿øÈ¿¼Ò½ÃÇè.
  • bacterium, purple sulfur
    ÀÚȲ¼¼±Õ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • oxygenase
    ¿Á½ÃÀú³×À̽º
  • coenzyme Q-cytochrome c reductase complex
    º¸È¿¼Ò(ÜÍý£áÈ) Q¡¤»çÀÌÅäÅ©·Ò C ¸®´ÚÅ×À̽º (ÔÒ) complex III
  • dihydrofolate reductase
    ÀÌ(ì£)¼ö¼Ò(â©áÈ)Æú»ê(ß«) ¸®´öÅ×À̽º
  • folic acid reductase
    Æú»ê(ß«) ¸®´ÚÅ×À̽º
  • iron-sulfur cluster
    ö-À¯È²(ôÑ×¼üÜ) ¹¶Ä¡
  • iron-sulfur protein
    ö-À¯È² ´Ü¹éÁú(ôÑ×¼üÜÓ±ÛÜòõ)
  • labile sulfur
    ºÒ¾ÈÁ¤ Ȳ(ÝÕäÌïÒüÜ)
  • nitrate reductase
    Áú»ê(òòß«) ¸®´ÚÅ×À̽º
  • nitrite reductase
    ¾ÆÁú»ê(ä¬òòß«)¸®´ÚÅ×À̽º
  • purple sulfur bacteria
    ÀÚ»ö Ȳ¼¼±Õ(í¹ßäüÜá¬Ð¶)
  • reductase
    "¸®´ÚÅ×À̽º, ȯ¿øÈ¿¼Ò(ü½êªý£áÈ)"
  • ribonucleotide reductase
    ¶óÀ̺¸´ºÅ¬¸®¿ÀŸÀÌµå ¸®´ÚÅ×À̽º
  • succinate-coenzyme Q reductase
    ¼÷½Å»ê(ß«)-º¸È¿¼Ò(ÜÍý£áÈ)Q ¸®´ÚÅ×À̽º
  • sulfur
    Ȳ(üÜ)
  • sulfur amino acid
    Ȳ(üÜ)¾Æ¹Ì³ë»ê(ß«)
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • sulfur colloid
    Ȳ±³Áú
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
ASF African swine fever; aniline-sulfur-formaldehyde [resin]
Fe/S iron/sulfur [protein]
TSC technetium sulfur colloid; thiosemicarbazide; transverse spinal sclerosis; tuberous sclerosis
TST thiosulfate sulfur-transferase; thromboplastin screening test; total sleep time; transforming sequen...
HMOX heme oxygenase
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
HMG-CoA reductase 3-Hydroxy-3-methylglutaryl CoA reductase
HMG-CoA reductase 3-Hydroxy-3-methylglutaryl coenzyme A reductase
HiPIP High Potential Iron-sulfur Protein
S Sulfur
SF6 Sulfur Hexa Fluoride
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 10 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • acetaldehyde reductase
    ¾Æ¼¼Æ® ¾Ëµ¥ÇÏÀ̵å ȯ¿ø È¿¼Ò
  • oxygenase
    ¿Á½Ã°Ô³ªÁ¦
    »ê¼Ò ÷°¡ È¿¼Ò. ºÐÀÚ»ó »ê¼ÒÀÇ 2¿øÀÚ¸¦ ±âÁú¿¡ °áÇÕ½ÃŰ´Â °ÍÀ» Ã˸ÅÇÏ´Â »êÈ­ ȯ¿ø È¿¼ÒÀÇ Á¾·ù
  • sulfur bacteria
    Ȳ ¼¼±Õ
    Ȳ ¶Ç´Â ¹«±â È­ÇÕ¹°À» »êÈ­ÇÔÀ¸·Î½á ¹ßÀ°¿¡ ÇÊ¿äÇÑ ¿¡³ÊÁö¸¦ ¾ò´Â ¼¼±Õ. Ȳõ, ¿À¼ö, Åä¾ç Áß¿¡ »ýÀ°ÇÑ´Ù. Ȳ, Ȳȭ ¼ö¼Ò ¹× ´Ù¸¥ Ȳȭ¹°, ¾ÆÈ²»ê¿°·ù, Ƽ¿À Ȳ»ê¿° µîÀ» »êÈ­Çϰí, ¶Ç´Â ¼ö¼Ò ÀÌÅ»À» ÇàÇϰųª ź»ê ¹«¼ö¹°À» µ¿È­ÇÏ¿© Áõ½ÄÇϸç, ±× ¿µ¾ç¿¡ À¯±â ź¼Ò È­ÇÕ¹°À» ÇÊ¿ä·Î ÇÏÁö ¾Ê´Â ¼¼±ÕÀÌ´Ù. Ȳ ¼¼±Õ¿¡´Â ¹«»ö Ȳ ¼¼±Õ
  • sulfur balsam
    Ȳ ¹ß»ï
  • sulfur cycle
    Ȳ ¼øÈ¯
  • sulfur dioxide control
    ÀÌ»êÈ­ Ȳ °¡½º ±ÔÁ¦
  • sulfur flower
    Ȳȭ
  • sulfur point
    Ȳ ºñÁ¡
  • sulfur recovery
    À¯È² ȸ¼ö
  • sulfur-containing amino acid
    Ȳ ÇÔÀ¯ ¾Æ¹Ì³ë»ê
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
sulfur oxygenase reductase <enzyme> From desulfurolobus ambivalens; in the presence of oxygen but not under a hydrogen atmosphere simultaneously produces sulfite, thiosulfate, and hydrogen sulfide from sulfur; inhibited by sulfhydryl reagents, fad, ferrous and ferric ions
Registry number: EC 1.8.-
Synonym: sor gene product (sulfur oxygenase reductase)
(26 Jun 1999)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
sulfur-sulfur bond isomerases <enzyme> Enzymes that catalyze the transposition of a sulfur-sulfur bond.
Registry number: EC 5.3.4
(12 Dec 1998)
phthalate oxygenase reductase <enzyme> Flavoenzyme which transfers electrons from NADH to the iron-sulfur centre of phthalate oxygenase
Registry number: EC 1.-
Synonym: phthalate dioxygenase reductase
(26 Jun 1999)
alpha-ketoisocaproate oxygenase <enzyme> From rat liver cytosol; oxidatively decarboxylates and hydroxylates alpha-ketoisocaporate to form beta-hydroxyisovalerate; requires fe(2+) and thiol; activated by ascorbate
Registry number: EC 1.13.11.-
Synonym: 2-ketoisocaproate oxygenase, alpha-ketoisocaproate dioxygenase
(26 Jun 1999)
anhydrotetracycline oxygenase <enzyme> Streptomyces aureofaciens enzyme catalyzing penultimate reaction of tetracycline biosynthesis, hydration of anhydrotetracycline to dehydrotetracycline
Registry number: EC 1.14.99.-
(26 Jun 1999)
aniline oxygenase <enzyme> Converts substituted anilines to the corresponding catechols
Registry number: EC 1.14.99.-
(26 Jun 1999)
benzene mono-oxygenase <enzyme> Cytochrome p-450-dependent; forms benzene oxide
Registry number: EC 1.13.12.-
(26 Jun 1999)
bromomethane mono-oxygenase <enzyme> Enzyme responsible for methane oxidation in vivo
Registry number: EC 1.13.12.-
(26 Jun 1999)
ribulose-1,5-bisphosphate carboxylase-oxygenase large subunit epsilonN-methyltransferase <enzyme> An aspect of EC 2.1.1.43; trimethylates lys-14 of rubisco
Registry number: EC 2.1.1.-
Synonym: rubisco lsmt, rubisco large subunit lysine n-methyltransferase
(26 Jun 1999)
ribulosebisphosphate carboxylase-oxygenase activase <chemical> Requires ATP; amino acid sequence given in first source
Synonym: rubisco activase, rca protein
(26 Jun 1999)
porphobilinogen oxygenase <enzyme> Porphobilinogen is converted to 5-oxo-porphobilinogen
Registry number: EC 1.13.-
(26 Jun 1999)
haem oxygenase (decyclizing) <enzyme> A mixed function oxidase enzyme which during haemoglobin catabolism catalyses the degradation of haem to ferrous iron, carbon monoxide and biliverdin in the presence of molecular oxygen and reduced NADPH. The enzyme is induced by metals, particularly cobalt.
Chemical name: Haem,hydrogen-donor:oxygen oxidoreductase (alpha-methene-oxidizing, hydroxylating)
Registry number: EC 1.14.99.3
(12 Dec 1998)
cyclohexanone oxygenase <enzyme> Requires NADPH and oxygen, forms epsilon-caprolactone
Registry number: EC 1.14.13.-
Synonym: cyclohexanone monooxygenase, flavoenzyme cyclohexanone monooxygenase
(26 Jun 1999)
dihydroxynaphthalene oxygenase <enzyme> Also catalyses ring cleavage in an extradiol mode: between a hydroxylated and an adjacent non-hydroxylated carbon
Registry number: EC 1.13.-
Synonym: 1,2-dihydroxynaphthalene dioxygenase
(26 Jun 1999)
questin oxygenase <enzyme> Catalyses the conversion of questin to desmethylsulochrin; isolated from aspergillus terreus
Registry number: EC 1.14.13.-
(26 Jun 1999)
oxygenase <enzyme> That catalyses the incorporation of the oxygen of molecular oxygen into organic substrates. Dioxygenases (oxygen transferases) catalyse introduction of both atoms of molecular oxygen, monoxygenases (mixed function oxygenases) introduce one atom, the other becomes reduced to water, so that these enzymes require a second substrate, acting as oxygen donor. Both types are used by bacteria in degradation of aromatic compounds. Dioxygenases all contain iron, for example tryp 2, 3 dioxygenase.
Examples of mono oxygenases are the enzymes that hydroxylate proline and lysine of collagen, using ketoglutarate.
(18 Nov 1997)
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 4 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • oxygenase
    »ê¼Ò ÷°¡(»ê¼ÒÈ­)È¿¼Ò;¿Á½Ã°Ô³ª¾ÆÁ¦
  • reductase
    ȯ¿øÈ¿¼Ò
  • sulfur
    À¯È²
  • sulfur
    na;À¯È²(»öÀÇ);Ȳ³ì»ö(ÀÇ)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
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    ±¸ºÐ/º¸Çè±Þ¿©
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    ±¸ºÐ/º¸Çè±Þ¿©
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