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"proline oxidase"¿¡ ´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®
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  • proline
    ÇÁ·Ñ¸°
  • labile oxidase reaction
    ºÒ¾ÈÁ¤»êÈ­È¿¼Ò¹ÝÀÀ
  • oxidase
    »êÈ­È¿¼Ò
  • oxidase reaction
    »êÈ­È¿¼Ò¹ÝÀÀ
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  • ¿µ¹®
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  • oxidase
    »êÈ­È¿¼Ò
  • proline
    ÇÁ·Ñ¸°
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  • ¿µ¹®
    ÇѱÛ
  • proline
    ÇÁ·Ñ¸°
  • cytochrome oxidase test
    ½ÃÅäÅ©·Ò»êÈ­È¿¼Ò°Ë»ç
  • oxidase
    »êÈ­È¿¼Ò
  • oxidase reaction
    »êÈ­È¿¼Ò¹ÝÀÀ
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  • ¿µ¹®
    ÇѱÛ
  • proline
    ÇÁ·Ñ¸°.
  • GOD= glucose oxidase
    Æ÷µµ´ç»êÈ­ È¿¼Ò.
  • Kovacs oxidase reagent
    Äڹ齺 »êÈ­È¿¼Ò°Ë»ç½Ã¾à
  • MAO=£¾monoamine oxidase
    ¸ð³ë¾Æ¹Î»ê È­È¿¼Ò.
  • NADPH-dependent oxidase system
    NADPH-ÀÇÁ¸¼º »êÈ­È¿¼Ò°è
  • glucose oxidase
    Æ÷µµ´ç»êÈ­È¿¼Ò
  • glucose oxidase =GOD
    ±Û·çÄÚ¿À½º »êÈ­È¿¼Ò(¡­ß«ûùý£áÈ), ±Û·çÄÚ¿À½º¿Á½Ã ´ÙÁ¦.
  • histamine oxidase
    È÷½ºÅ¸¹Î¿Á½Ã´ÙÁ¦.
  • homogentisic acid oxidase
    È£¸ð°ÕƼ½Å»ê »êÈ­È¿¼Ò(¡­ß«ß«ûùý£áÈ).
  • homogentisic acid oxidase
    È£¸ð°ÕƼ½Å»ê»êÈ­È¿¼Ò
  • homogentisic oxidase
    È£¸ð°ÕƼ½Å»ê(Homogentisin) »êÈ­È¿¼Ò
  • indophenol oxidase
    ÀεµÆä³î»êÈ­È¿¼Ò.
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  • ¿µ¹®
    ÇѱÛ
  • proline
    ÇÁ·Ñ¸°.
  • benzidine oxidase
    º¥Áöµò»êÈ­È¿¼Ò
  • cysteine oxidase
    ½Ã½ºÅ×ÀλêÈ­È¿¼Ò(¡­ß«ûùý£áÈ).
  • cytochrome C oxidase deficiency
    ½ÃƮũ·Ò C ¿Á½Ã´ÙÁ¦(»êÈ­È¿¼Ò)°áÇÌ
  • cytochrome oxidase
    »çÀÌÅäÅ©·Ò ¿Á½Ãµ¥À̽º, »êÈ­È¿¼Ò(ß«ûùý£áÈ) .
  • cytochrome oxidase
    »çÀÌÅäÅ©·Ò»êÈ­¿ä¼Ò
  • cytochrome oxidase test
    »çÀÌÅäÅ©·Ò »êÈ­È¿¼Ò °Ë»ç
  • diamine oxidase
    µð¾Æ¹Î»êÈ­È¿¼Ò(¡­ß«ûù ý£áÈ).
  • dopa-oxidase
    µµÆÄ»êÈ­È¿¼Ò(¡­ß«ûùý£áÈ).
  • glucose oxidase
    Æ÷µµ´ç»êÈ­È¿¼Ò
  • glucose oxidase =GOD
    ±Û·çÄÚ¿À½º »êÈ­È¿¼Ò(¡­ß«ûùý£áÈ), ±Û·çÄÚ¿À½º¿Á½Ã ´ÙÁ¦.
  • histamine oxidase
    È÷½ºÅ¸¹Î¿Á½Ã´ÙÁ¦.
  • homogentisic acid oxidase
    È£¸ð°ÕƼ½Å»ê»êÈ­È¿¼Ò
  • homogentisic acid oxidase
    È£¸ð°ÕƼ½Å»ê »êÈ­È¿¼Ò(¡­ß«ß«ûùý£áÈ).
  • homogentisic oxidase
    È£¸ð°ÕƼ½Å»ê(Homogentisin) »êÈ­È¿¼Ò
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  • ¿µ¹®
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  • proline
    ÇÁ·Ñ¸°
  • amino acid oxidase
    ¾Æ¹Ì³ë»ê(ß«) ¿Á½Ãµ¥À̽º
  • cholesterol oxidase
    ÄÝ·¹½ºÅ×·Ñ ¿Á½Ãµ¥À̽º
  • cytochrome c oxidase complex
    »çÀÌÅäÅ©·Ò c ¿Á½Ãµ¥À̽º º¹ÇÕü(ÜÜùêô÷) (ÔÒ) complex IV
  • cytochrome oxidase
    »çÀÌÅäÅ©·Ò ¿Á½Ãµ¥À̽º
  • mixed function oxidase
    È¥ÇÕ±â´É(ûèùêѦÒö)¿Á½Ãµ¥À̽º
  • monoamine oxidase
    ¸ð³ë¾Æ¹Î ¿Á½Ãµ¥À̽º
  • oxidase
    "¿Á½Ãµ¥À̽º, »êÈ­È¿¼Ò(ß«ûùý£áÈ)"
  • sulfite oxidase deficiency
    ¾ÆÈ²»ê(ä¬üÜß«) ¿Á½Ãµ¥À̽º °áÇÌ(ÌÀù¹)
  • ubiquinol : cytochrome C oxidase
    À¯ºñÄû³î:»çÀÌÅäÅ©·Ò C ¿Á½Ãµ¥À̽º
  • urate oxidase
    ´¢»ê¿°(Òãß«ç¤) ¿Á½Ãµ¥À̽º
  • xanthine oxidase
    À鯾 ¿Á½Ãµ¥À̽º
  • xathine oxidase factor
    À鯾 ¿Á½Ãµ¥À̽º ÀÎÀÚ(ì×í­)
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  • ¿µ¹®
    ÇѱÛ
  • oxidase
    »êÈ­È¿¼Ò, ¿Á½Ã´ÙÁ¦
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PAO peak acid output; peripheral airway obstruction; plasma amine oxidase; polyamine oxidase; pulmonary ...
APRP acidic proline-rich protein; acute phase reactant protein
PPH past pertinent history; persistent pulmonary hypertension; phosphopyruvate hydratase; postpartum hem...
PRB basic proline-rich protein; Prosthetics Research Board
Pro proline; prophylactic; prothrombin
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
DHP 3,4,dehydro-D,L-proline
PRO L-proline
PRP Proline-Rich Polypeptides
PDPK Proline-directed protein kinase
PYK2 Proline-rich Tyrosine Kinase-2
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • cytochrome oxidase test
    »çÀÌÅäÅ©·Ò »êÈ­ È¿¼Ò °Ë»ç
  • histamine oxidase
    È÷½ºÅ¸¹Î ¿Á½Ã´ÙÁ¦
  • mixed function oxidase
    È¥ÇÕ ±â´É ¿Á½Ãµ¥À̽º
  • monoamine oxidase
    ¸ð³ë ¾Æ¹Î »êÈ­ È¿¼Ò, ¸ð³ë¾Æ¹Î ¿Á½Ã´ÙÁ¦
  • NADPH oxidase NADPH+2O2=NADP+ +2O2-ÀÇ È­ÇйÝÀÀÀ» Ã˸ÅÇÏ´Â »êÈ­ ȯ¿ø È¿¼ÒÀÇ ÇÑ Á¾·ùÀÌ´Ù. ÀÌ È¿¼Ò°èÀÇ À¯ÀüÀû °áÇÌÀº ¸¸¼º À°¾ÆÁ¾¼º ÁúȯÀ» À¯¹ßÇÑ´Ù.

    Nadsonieae

    ³ªµå¼Ò´Ï¾ÆÁ·
    È¿¸ð±Õ¾Æ°ú SaccharomycetoideaeÀÇ 1Á·À¸·Î, ±Õ»ç°¡ ¾ø°í, ·¹¸ó¸ð¾çÀÇ ºÐ¾Æ¼¼Æ÷°¡ ¹ß»ýÇÑ´Ù.
  • oxidase reaction
    »êÈ­ È¿¼Ò ¹ÝÀÀ
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
proline oxidase <enzyme> The first enzyme of the proline degradative pathway. It catalyses the oxidation of proline to pyrroline-5-carboxylic acid in the presence of oxygen and water. The action is not reversible. The specific activity of proline oxidase increases with age.
Registry number: EC 1.5.3.-
(12 Dec 1998)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
procollagen-proline dioxygenase <enzyme> A mixed-function oxygenase that catalyses the hydroxylation of a prolyl-glycyl-containing-peptide, usually in protocollagen, to a hydroxyprolylglycyl-containing-peptide. The enzyme utilises molecular oxygen with a concomitant oxidative decarboxylation of 2-oxoglutarate to succinate.
Chemical name: Procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase
Registry number: EC 1.14.11.2
(12 Dec 1998)
proline <amino acid> One of the 20 amino acids directly coded for in proteins. Structure differs from all the others, in that its side chain is bonded to the nitrogen of the _ amino group, as well as the _ carbon. This makes the amino group a secondary amine and so proline is described as an imino acid. Has strong influence on secondary structure of proteins and is much more abundant in collagens than in other proteins, occurring especially in the sequence glycine proline hydroxyproline. A proline rich region seems to characterise the binding site of SH3 domains.
(18 Nov 1997)
proline, 2-oxoglutarate 3-dioxygenase <enzyme> Prolyl 3-hydroxylase is separate enzyme from prolyl 4-hydroxylase; catalyses post translational modification of collagen
Registry number: EC 1.14.11.7
Synonym: proline 3-hydroxylase, prolyl 3-hydroxylase
(26 Jun 1999)
proline aminopeptidase A hydrolase cleaving l-proline residues from the N-terminal position in peptides.
Synonym: proline aminopeptidase.
(05 Mar 2000)
proline-beta-naphthylamidase <enzyme> From pig intestinal mucosa; hydrolyzes proline-beta-naphthylamidase; distinct from proline aminopeptidase; inhibited by active site serine-specific protease inhibitors
Registry number: EC 3.4.11.-
Synonym: pro-naphthylamidase
(26 Jun 1999)
proline dehydrogenase An oxidoreductase reducing 1-pyrroline-2-carboxylate to l-proline with NAD(P)H.
Synonym: proline dehydrogenase, proline oxidase.
(05 Mar 2000)
proline dipeptidase <enzyme> An enzyme cleaving aminoacyl-l-proline bonds in dipeptides containing a C-terminal prolyl residue; a deficiency of this enzyme results in hyperimidodipeptiduria.
Synonym: imidodipeptidase, peptidase D, prolidase.
(05 Mar 2000)
proline iminopeptidase A hydrolase cleaving l-proline residues from the N-terminal position in peptides.
Synonym: proline aminopeptidase.
(05 Mar 2000)
proline permease <chemical> Prnb isolated from aspergillus nidulans
Chemical name: permease, proline
Synonym: l-proline permease, proline porter, proline transporter, putp gene product, sodium-proline permease, na(+)-proline permease, prnb gene product
(26 Jun 1999)
proline racemase <enzyme> An enzyme that reversibly converts d-proline to l-proline.
(05 Mar 2000)
proline-specific dipeptidylcarboxypeptidase <enzyme> From streptomyces species; removes diproline form c-terminus of proline-containing peptides such as boc-pro-pro-pro-pro or leu-pro-pro-pro-pro-pro
Registry number: EC 3.4.15.-
Synonym: pro-dpp-carboxypeptidase
(26 Jun 1999)
protein-proline kinase <enzyme> Phosphorylates synapsin i; phosphorylation takes place on serine 20, which is flanked by two proline molecules; heterodimer of p34(cdc2)/p58(cyclin a)
Registry number: EC 2.7.10.-
Synonym: proline-directed protein kinase
(26 Jun 1999)
SH3 domain-containing proline-rich kinase <enzyme> A protein kinase which both phosphorylates ser and thr residues and has an sh3 domain; contains 847 amino acid residues; mol mass 92,688 da; genbank u07747
Registry number: EC 2.7.10.-
Synonym: src-homology 3 domain-containing proline-rich kinase, sprk protein, sprk gene product
(26 Jun 1999)
d-proline reductase An oxidoreductase reversibly reacting d-proline with NADH to produce 5-aminovalerate and NAD+.
(05 Mar 2000)
acetaldehyde oxidase <enzyme> Acetaldehyde is converted to acetate
Registry number: EC 1.2.-
(26 Jun 1999)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 1 ÆäÀÌÁö: 1
  • Proline Oxidase - »õâ The first enzyme of the proline degradative pathway. It catalyzes the oxidation of proline to pyrroline-5-carboxylic acid in the presence of oxygen and water. The action is not reversible. The specific activity of proline oxidase increases with age. EC 1.5.3.-.
    Synonyms : Dehydrogenase, Proline, Oxidase, Proline
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proline oxidase proline dehydrogenase.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
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