¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"2,3-dihydroxybenzoate - serine ligase"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • ligase
    ¿¬°áÈ¿¼Ò, ¶óÀ̰ÔÀ̽º
  • serine
    1. ¼¼¸° 2. ¼¼¸°Á¦
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • serine
    ¼¼¸°
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • ligase
    ¿¬°áÈ¿¼Ò, °áÇÕÈ¿¼Ò
  • serine
    ¼¼¸°
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • DNA ligase
    DNA ¿¬°áÈ¿¼Ò
  • phosphatidyl serine
    Æ÷½ºÆÄƼµô¼¼¸°
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 4 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • ligase
    ¿¬°áÈ¿¼Ò(ææÌ¿ý£áÈ), ¶óÀ̰ÔÀ̽º.
  • ligase
    ¿¬°áÈ¿¼Ò, °áÇÕÈ¿¼Ò
  • phosphatidyl serine
    Æ÷½ºÆÄƼµô¼¼¸°
  • serine
    ¼¼¸°
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 13 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • phosphatidal serine
    Æ÷½ºÆÄƼ´Þ ¼¼¸°
  • serine
    ¼¼¸°
  • serine convention
    ¼¼¸° ¹æ½Ä(Û°ãÒ)
  • serine esterase
    ¼¼¸° ¿¡½ºÅÍ·¹À̽º
  • serine protease
    ¼¼¸° ÇÁ·ÎƼ¿¡À̽º
  • acid-ammonia ligase
    »ê(ß«)¾Ï¸ð´Ï¾Æ ¶óÀ̰ÔÀ̽º
  • acid-thiol ligase
    »ê(ß«)ŸÀ̿öóÀ̰ÔÀ̽º
  • DNA ligase
    DNA ¶óÀ̰ÔÀ̽º
  • fatty acid CoA ligase
    Áö¹æ»ê(ò·Û¸ß«) CoA ¶óÀ̰ÔÀ̽º
  • ligase
    ¶óÀ̰ÔÀ̽º
  • polynucleotide ligase
    Æú¸®´©Å¬·¹¿ÀŸÀÌµå ¶óÀ̰ÔÀ̽º
  • RNA ligase
    RNA ¶óÀ̰ÔÀ̽º
  • T4 RNA ligase
    T4 RNA ¶óÀ̰ÔÀ̽º
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
FACL fatty acid coenzyme ligase
GLUL glutamate (ammonia) ligase
CAAX [box] protein segment in which C is cysteine, A is usually but not always an aliphatic amino acid, and X i...
HFSP Hanukah factor serine protease
PS pacemaker syndrome; paired stimulation; paradoxical sleep; paraspinal; parasympathetic; Parkinson sy...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
4CL 4-Coumarate:coenzyme A ligase
LCR Ligase Chain Reaction
Ser L-serine
L-SOP L-serine O-phosphate
SDH L-serine dehydratase
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • serine
    ¼¼¸°
    1. ´Ü¹éÁúÀ» ±¸¼ºÇÏ´Â ¾Æ¹Ì³ë»êÀÇ Çϳª. ´ë»çµÇ¾î ÇǸ£ºó»êÀ¸·Î µÈ´Ù. 2. õ¿¬À¸·Î Á¸ÀçÇÏ´Â ºñÇʼö ¾Æ¹Ì³ë»ê. C3H7NO3. ±Û¶óÀ̽ſ¡¼­ ÇÕ¼ºµÈ´Ù.
  • serine esterase
    ¼¼¸° ¿¡½ºÅ×¶ó¾ÆÁ¦
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
2,3-dihydroxybenzoate - serine ligase <enzyme> From E coli; ATP and 2,3-dihydroxybenzoate and serine yields the products of ATP breakdown and n-(2,3-dihydroxybenzoyl)-l-serine; involved in biosynthesis of enterobactin
Registry number: EC 6.3.2.14
Synonym: enterochelin synthetase, entf gene product, 2,3-dihydroxybenzoylserine synthetase
(26 Jun 1999)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
serine-trna ligase <enzyme> An enzyme that activates serine with its specific transfer RNA.
Chemical name: L-Serine:tRNA(Ser) ligase (AMP-forming)
Registry number: EC 6.1.1.11
(12 Dec 1998)
amyloid A-degrading serine protease <enzyme> Reduced in amyloidosis associated with rheumatoid arthritis
Registry number: EC 3.4.21.-
Synonym: amyloid a-degrading activity, aad-protease
(26 Jun 1999)
atrial granule serine proteinase <enzyme> Converts pro-atrial natriuretic factor to anf by cleaving the arg98-ser99 bond; n-terminal 26-residue amino acid sequence given in first source
Registry number: EC 3.4.21.-
(26 Jun 1999)
p57 serine proteinase <enzyme> From membranes of human erythrocytes; cleaves c3, the third component of complement; mw 57 kD; 20 first n-terminal residues 100% homologous to residues 910-929 of human erythrocyte ankyrin; n-terminal sequence given in first source
Registry number: EC 3.4.21.-
Synonym: p57 membrane serine proteinase, erythrocyte p57 proteinase
(26 Jun 1999)
VCP1 serine protease <enzyme> Isolated from verticillium chlamydosporium
Registry number: EC 3.4.21.-
(26 Jun 1999)
MBP-associated serine protease <enzyme> Genbank d28593
Registry number: EC 3.4.21.-
Synonym: masp protease, mannose-binding protein-associated serine protease
(26 Jun 1999)
cdpdiacylglycerol-serine o-phosphatidyltransferase <enzyme> An enzyme that catalyses the formation of phosphatidylserine and cmp from cdpdiglyceride plus serine.
Chemical name: CDPdiacylglycerol:L-serine 3-O-phosphatidyltransferase
Registry number: EC 2.7.8.8
(12 Dec 1998)
MTSP-1 serine protease <enzyme> 29-kD protease isolated from mouse spleen; n-terminal
Registry number: EC 3.4.21.-
Synonym: mouse trypsin-type serine protease 1
(26 Jun 1999)
MTSP-2 serine protease <enzyme> 29-kD protein isolated from mouse spleen
Registry number: EC 3.4.21.-
Synonym: mouse trypsin-type serine protease 2
(26 Jun 1999)
myelencephalon-specific serine protease <enzyme> Specifically expressed in the nervous system; plays a role in normal homeostasis and response of spinal cord to injury.
Registry number: EC 3.4.21.-
Synonym: myelencephalon-specific protease, msp enzyme
(26 Jun 1999)
PP5 protein-serine-threonine phosphatase <enzyme> Has 4 tetratricopeptide repeat (tpr) motifs; similar to ppt1 protein; do not confuse with the placental protein pp5; amino acid sequence given in first source
Registry number: EC 3.1.3.-
Synonym: pp5 phosphatase, protein phosphatase 5
(26 Jun 1999)
Pr1 serine protease <enzyme> Isolated from verticillium chalmydosporium
Registry number: EC 3.4.21.-
(26 Jun 1999)
cytotoxic T lymphocyte-specific serine protease <enzyme> Structural sequence given in first source
Registry number: EC 3.4.21.-
Synonym: cytotoxic t lymphocyte-specific serine protease ccp I, cytotoxic t lymphocyte specific serine protease ccp II, mast cell protease type II
(26 Jun 1999)
protein-serine-threonine kinases <enzyme> A group of enzymes that catalyses the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
Registry number: EC 2.7.10
(12 Dec 1998)
protein-serine-threonine phosphatase <enzyme> Consider also EC 3.1.3.16 phosphoprotein phosphatases
Registry number: EC 3.1.3.-
Synonym: serine phosphatase, threonine phosphatase, protein-serine phosphatase, serine-threonine phosphatase
(26 Jun 1999)
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • ligase
    ¸®°¡Á¦(ÇÙ»ê ºÐÀÚ¸¦ °áÇÕÇÏ´Â È¿¼Ò)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 1
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 1
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ À¯»ç °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 1
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference ¸ÂÃã °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 1
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 1
ÅëÇÕ°Ë»ö ¿Ï·á