| ¿µ¹® | deoxyribonucleic acid (DNA) | ÇÑ±Û | µ¥¿Á½Ã¸®º¸ÇÙ»ê |
|---|---|---|---|
| ¼³¸í | ÇÙ»êÀÇ ÀÏÁ¾À¸·Î DNA¶ó°íµµ ÇÑ´Ù. DeoxyribonucleotideÀÇ ÁßÇÕüÀ̸ç À¯ÀüÀÚÀÇ ÈÇÐÀû º»Ã¼ÀÌ´Ù. RNA¹ÙÀÌ·¯½º ÀÌ¿ÜÀÇ ¸ðµç »ý¹°Àº DNA¸¦ À¯ÀüÀÚ·Î Áö´Ï°í ÀÖ´Ù. µð¿Á½Ã¸®º¸´ºÅ¬·¹¿ÀƼµå(deoxyribonucleotide)´Â ¿°±â¿Í ´ç(2'-deoxy-D-ribose)°ú ÀλêÀ¸·Î ÀÌ·ç¾îÁø´Ù. ¿°±â´Â ¾Æµ¥´Ñ(adenine), ±¸¾Æ´Ñ(guanine), Ƽ¹Î(thymine)¹× ½ÃÅä½Å(cytosine)ÀÇ 4°¡ÁöÀ̸ç, À̰ÍÀº ´ç¿¡ ºÎÂøµÇ¾î ÀÖ´Ù. ÀÎ»ê ¿ª½Ã ´çÀÇ ÇÑ ºÎºÐ¿¡ ºÎÂøµÇ¾î ÀÖ´Ù. ÀÌ deoxyribonucleotideÀÇ ´çÀº ´Ù¸¥ deoxy- ribonucleotideÀÇ ´ç°ú ÀλêÀ» »çÀÌ¿¡ ³õ°í °áÇÕÀ» ÇÏ°Ô µÇ¾î ÇϳªÀÇ ±ä »ç½½À» Çü¼ºÇÏ°Ô µÈ´Ù. Áï ´ç°ú ÀλêÀÌ ÁÖÃàÀÌ µÇ¾î¼ deoxyribonucleotideÀÇ ±ä »ç½½À» ¸¸µç´Ù. ÀÌ deoxyribonucleotideÀÇ »ç½½ µÎ °³´Â °¢°¢ deoxyribonucleotide¿¡ ºÎÂøµÇ¾î ÀÖ´Â ¿°±âµéÀÌ °áÇÕÀ» ÇÏ¿© µÎ °³ÀÇ »ç½½ÀÌ °áÇյǾî ÀÖ´Â ÀÌÁß³ª¼± ±¸Á¶¸¦ ¸¸µé°Ô µÈ´Ù. 4°¡Áö ¿°±â ¾Æµ¥´ÑÀº Ƽ¹Î°ú °áÇÕÀ» Çϰí, ½ÃÅä½Å°ú °áÇÕÀ» ÇÏ°Ô µÈ´Ù. Áï ´ç°ú ÀλêÀº ±ä »ç½½À» ¸¸µå´Â ¿ªÇÒÀ» ÇÏ°í ±ä »ç½½¿¡ ºÎÂøµÈ ¿°±âµéÀÇ °áÇÕ¿¡ ÀÇÇØ¼ µÎ °³ÀÇ ±ä »ç½½Àº ¼·Î ºÙ¾î¼ ÀÌÁß³ª¼± ±¸Á¶¸¦ ¸¸µç´Ù. DNAÀÇ À¯ÀüÁ¤º¸´Â ¿°±â¿¡ ÀúÀåµÈ´Ù. 4°³ÀÇ ¿°±âÀÇ Á¶ÇÕ°ú ¹è¿ÀÌ À¯ÀüÁ¤º¸¸¦ º¸°üÇÏ´Â ÇϳªÀÇ ¾ÏÈ£ ¿ªÇÒÀ» ÇàÇÏ°Ô µÈ´Ù. |
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| ¿µ¹® | retinoic acid | ÇÑ±Û | ·¹Æ¼³ë»ê |
|---|---|---|---|
| ¼³¸í | C20H28O2. ºñŸ¹Î AÀÇ ¾ËÄڿñ⸦ ¾Ëµ¥È÷µå·Î »êÈÇÑ ÈÄ ´Ù½Ã Ä«¸£º¹½Ç»êÀ¸·Î »êÈÇÏ¿© ¾òÀº »ê. ¹ß»ýÁßÀÇ ¼¼Æ÷¿¡ ÀÛ¿ëÇÏ¿© ÇüŸ¦ ¸¸µå´Âµ¥ °ü¿©ÇÑ´Ù. |
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| ¿µ¹® | ribonucleic acid | ÇÑ±Û | ¸®º¸ÇÙ»ê |
|---|---|---|---|
| ¼³¸í | Ribonucleotide monomer·Î ÀÌ·ç¾îÁø ÇÙ»êÀ¸·Î ¿°±â, ´ç, ÀλêÀ¸·Î ±¸¼ºµÈ´Ù. ¿°±â´Â adenine, guanine, cytosine, uracilÀÇ 4Á¾·ù°¡ ÀÖÀ¸¸ç, ´çÀº 5ź´çÀÌ´Ù. RNA´Â DNA¸¦ ÁÖÇüÀ¸·Î ÇÏ¿© »óº¸ÀûÀ¸·Î °áÇÕ, Çü¼ºµÇ¸ç ´Ü¹éÁúÀ» ¸¸µé¾î³»´Â µ¥¿¡ ÀÖ¾î Áß¿äÇÑ ¿ªÇÒÀ» ÇÑ´Ù. Àü·É RNA(mRNA)´Â ´Ü¹éÁú ÇÕ¼º¿¡ ÀÖ¾î °¡Àå ±âº»ÀÌ µÇ´Â DNAÀÇ ¼¿À» »óº¸ÀûÀ¸·Î ¿Å°Ü ¹Þ¾Æ Àü´ÞÇÏ´Â Àü·É±¸½ÇÀ» ÇÏ´Â RNA. ¸®º¸¼Ø RNA(rRNA) ¸®º¸¼ØÀ» Çü¼ºÇÏ´Â 4°¡Áö RNA»ç½½(28S, 18S, 5.8S, 5S·Î ±¸¼º). Àü´Þ RNA(tRNA) ƯÁ¤ ¾Æ¹Ì³ë»êÀ» ÇÑÂÊ ³¡¿¡ Áö´Ï°í »óº¸Àû ¼¿ÀÇ mRNA¿Í ÀϽÃÀû °áÇÕÀ» ÀÌ·ç¸ç ´Ü¹éÁú ÇÕ¼º¿¡ Á÷Á¢ ±â¿©ÇÏ´Â RNAÀÌ´Ù. |
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| ¿µ¹® | acid | ÇÑ±Û | »ê |
|---|---|---|---|
| ¼³¸í | ¹°¿¡ ³ì¾ÒÀ» ¶§ ÀÌ¿ÂÈÇÏ¿© ¼ö¼Ò ÀÌ¿ÂÀ» ¸¸µå´Â ¹°Áú. ½Å¸ÀÀÌ ³ª°í û»ö ¸®Æ®¸Ó½º Á¾À̸¦ ºÓ°Ô º¯È½ÃŰ¸ç ¿°±â¿ÍÀÇ ÁßÈ ¹ÝÀÀ¿¡ ÀÇÇÏ¿© ¹°°ú ¿°À» ¸¸µé°í ÀÌ¿ÂÈ ¿¿¡¼ ¼ö¼Òº¸´Ù ¾Õ¿¡ ÀÖ´Â ±Ý¼Ó°ú ¹ÝÀÀÇÏ¿© ¿°À» ¸¸µé¸é¼ ¼ö¼Ò¸¦ ¹ß»ý½ÃŲ´Ù. ¼ö¼Ò ¿øÀÚ¸¦ ÀÌ¿ÂÈÇÏ´Â ÈûÀÇ °¾à¿¡ µû¶ó °»ê°ú ¾à»êÀ¸·Î ³ª´¶´Ù. |
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| ¿µ¹® | acetic acid | ÇÑ±Û | ¾Æ¼¼Æ®»ê, ÃÊ»ê |
|---|---|---|---|
| ¼³¸í | ºÐÀÚ½ÄÀº C2H4O2, ºÐÀÚ·® 60.05ÀÇ Àú±Þ Áö¹æ»êÀÌ´Ù. CH3COOHÀÇ ±¸Á¶½ÄÀ» °¡Áø ¹«»ö¾×ü·Î 16.7¡É¿¡¼ ³ì°í 118.0¡É¿¡¼ ²ú´Â´Ù. ½ÄÃÊÀÇ ½Å¸ÀÀ» ³»´Â °ÍÀ̰í, ³óÃàµÈ °ÍÀ» ºùÃÊ»êÀ̶ó ÇÑ´Ù. »ó¿Â¿¡¼´Â ¾×üÀÌ¸ç ¼ö¿ë¾×Àº ¾à»ê¼ºÀÌ´Ù. »ýü³»¿¡¼´Â ÀϹÝÀûÀ¸·Î ¾Æ¼¼Æ¿ CoA·Î Á¸ÀçÇÏ¸ç ¾Æ¼¼Æ¿±âÀÇ °ø±Þ¿øÀÌ µÇ´Â ¿Ü¿¡ Áö¹æ»êÀ̳ª ½ºÅ×·ÎÀÌµå µîÀÇ »ý¼ºÀç·á·Î Áß¿äÇÏ´Ù. ¾Æ¼¼Æ¿ CoA·ÎºÎÅÍ´Â ÄÉÅæÃ¼°¡ ÇÕ¼ºµÇ¸ç Á¶Á÷ÀÇ ¿¡³ÊÁö¿øÀÌ µÈ´Ù. |
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| NTA | natural thymocytotoxic autoantibody; nitrilotriacetic acid; Nurse Training Act |
|---|---|
| FMO | falvin-containing monooxygenase; Fleet Medical Officer; Flight Medical Officer |
| MMO | methane monooxygenase |
| PAM | pancreatic acinar mass; penicillin aluminum monostearate; peptidylglycine alpha-amidating monooxygen... |
| PHM | peptide histidine methionine; peptidylglycine alpha-hydroxylating monooxygenase; posterior hyaloid m... |
| AMO | Ammonia monooxygenase |
|---|---|
| DBM | Dopamine beta-monooxygenase |
| FMO | Flavin-containing monooxygenase |
| MMO | Methane monooxygenase |
| MO | Monooxygenase |
| nitrilotriacetic acid monooxygenase | <enzyme> Nadh and o2 required, forms ininodiacetic acid and glyoxylate Registry number: EC 1.7.- (26 Jun 1999) |
|---|
| nitrilotriacetic acid | <chemical> Chemical name: Glycine, N,N-bis(carboxymethyl)- (12 Dec 1998) |
|---|---|
| methanesulfonic acid monooxygenase | <enzyme> Catalyses conversion of methanesulfonic acid to formaldehyde and sulfite; requires NADH; consists of a, b, and c components; component c is an iron-sulfur protein Registry number: EC 1.14.13.- Synonym: msa monooxygenase, msmc component (26 Jun 1999) |
| quinaldic acid 4-monooxygenase | <enzyme> Catalyses conversion of quinaldic acid to kynurenic acid in presence of oxygen, iron(ii), and NADH; do not confuse with quinaldic acid 4-oxidoreductase Registry number: EC 1.14.13.- (26 Jun 1999) |
| lauric acid monooxygenase | <enzyme> Cytochrome p-450 linked, requires NADPH Registry number: EC 1.14.13.- Synonym: lauric acid hydroxylase, lauric acid omega-hydroxylase, lauric acid (omega-1)-hydroxylase, omega-1 hydroxylase, laurate omega-hydroxylase, cytochrome p-450iva1, cytochrome p450iva1, cytochrome p450iva3, cytochrome p-450iva3, omega-lauryl hydroxylase, cytochrome p-450 4a1, cytochrome p4504a1, cyp4a1, cyp4a, cytochrome p-450 4a, cyp4a2, cytochrome p-450 iva (26 Jun 1999) |
| acetone monooxygenase | <enzyme> Converts acetone to acetol and acetol to methylglyoxal Registry number: EC 1.14.13.- Synonym: acetol monooxygenase (26 Jun 1999) |
| alkane 1-monooxygenase | <enzyme> Alkb is an integral membrane protein component Registry number: EC 1.14.15.3 Synonym: alkane 1-hydroxylase, omega-hydroxylase, fatty acid omega-hydroxylase, alkyl monooxygenase, cytochrome p-450alk, cyp4a6, cyp4a7, cytochrome p-450ka2, cytochrome p450 4a11, cyp4a11, alkb gene product, pseudomonas oleovorans, alkb protein, alkb gene product, cyp4f4, cyp4f5 (26 Jun 1999) |
| alkene monooxygenase | <enzyme> Multicomponent, NADH or NADPH-dependent enzyme from mycobacterium; similar to EC 1.14.13.25 but only converts alkenes to the corresponding epoxides Registry number: EC 1.14.13.- (26 Jun 1999) |
| ammonia monooxygenase | <enzyme> Ammonia is oxidised to hydroxylamine by nitrifying bacterium, nitrosomonas europaea; also hydroxylates alkanes and arenes; converts alkenes to epoxides Registry number: EC 1.7.3.- Synonym: ammonia mono-oxygenase (26 Jun 1999) |
| anthranilate monooxygenase | <enzyme> Catalyses the hydroxylation of anthranilate to hydroxyanthranilate in the presence of tetrahydropteridine and molecular oxygen; anthranilate hydroxylase is a synonym for this and EC 1.14.12.1 and EC 1.14.13.35 (formerly EC 1.14.12.2) Registry number: EC 1.14.16.3 Synonym: anthranilate 3-hydroxylase, anthranilate 3-monooxygenase (26 Jun 1999) |
| arachidonate monooxygenase | <enzyme> Nadph-dependent enzyme from renal cortex; not inhibited by cyclooxygenase inhibitors; forms 19-hydroxyarachidonate, 20-hydroxyarachidonate, 19-ketoarachidonate and a dicarboxylic acid Registry number: EC 1.14.13.- (26 Jun 1999) |
| arginine 2-monooxygenase | <enzyme> Catalyses oxidative decarboxylation or arginine to form gamma-guanidinobutyramide (4-guanidinobutanamide) Registry number: EC 1.13.12.1 Synonym: arginine decarboxyoxidase (26 Jun 1999) |
| benzoyl-CoA 3-monooxygenase | <enzyme> A fad-dependent hydroxylase that hydroxylates benzoyl-CoA to 3-hydroxybenzoyl-CoA; mw 130 kD (composed of two identical subunits of 56 kD); from denitrifying pseudomonas sp. Registry number: EC 1.14.13.- Synonym: benzoyl-coenzyme a 3-monooxygenase (26 Jun 1999) |
| butadiene monooxygenase | <enzyme> P-450 dependent enzyme catalyzing epoxidation to butadiene monoxide Registry number: EC 1.14.- (26 Jun 1999) |
| camphor 5-monooxygenase | <enzyme> A monooxygenase haem-thiolate (cytochrome p-450) with camphor bound at the active site. It acts as the terminal monooxygenase in the d-camphor monooxygenase system. Under anaerobic conditions, this enzyme reduces the polyhalogenated compounds bound at the camphor-binding site. Additionally, it is the only cytochrome p-450 enzyme with a known crystal structure. Registry number: EC 1.14.15.1 (12 Dec 1998) |
| retinal monooxygenase | <enzyme> Cytochrome p-450 and NADPH-dependent enzyme from rabbit liver microsomes Registry number: EC 1.14.13.- Synonym: retinoic acid synthase (26 Jun 1999) |
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