¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"GDP-mannose mannosyl hydrolase"¿¡ ´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 : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • hydrolase
    °¡¼öºÐÇØÈ¿¼Ò
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 3 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • Glycerol ester hydrolase
    ±Û¸®¼¼·Ñ ¿¡½ºÅÍ °¡¼öºÐÇØÈ¿¼Ò(Ê¥â©ÝÂú°ý£áÈ)
  • aspartylglycosamine amide hydrolase, deficiency
    Aspartylglycosamine amide hydrolase°áÇÌ(¡­ÌÀù¹)
  • hydrolase
    ÇÏÀ̵å·Ñ·¹À̽º, Hydrolase
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 3 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • aspartylglycosamine amide hydrolase, deficiency
    Aspartylglycosamine amide hydrolase°áÇÌ(¡­ÌÀù¹)
  • hydrolase
    ÇÏÀ̵å·Ñ·¹À̽º, Hydrolase
  • peptidyldipeptide hydrolase
    ÆéƼµôµðÆéƼµåÈ÷µå·Ñ¶óÁ¦
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • alkaline hydrolase
    ¾ËÄ®¸®¼º ÇÏÀ̵å·Ñ·¹À̽º
  • hydrolase
    ÇÏÀ̵å·Ñ·¹À̽º
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
ACEH acid cholesterol ester hydrolase
CEH cholesterol ester hydrolase
DPH Department of Public Health; diphenhydramine; diphenylhexatriene; diphenylhydantoin; Diploma in Publ...
FGH formylglutathione hydrolase
GEH glycerol ester hydrolase
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
BH Bleomycin hydrolase
CEH Cholesterol ester hydrolase
cEH Cytosolic epoxide hydrolase
EH Epoxide hydrolase
FAAH Fatty acid amide hydrolase
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • hydrolase
    °¡¼öºÐÇØ È¿¼Ò, ÇÏÀ̵å·Ñ·¹À̽º
    ¿¡½ºÅÍ, ÆéŸÀ̵å, ±Û¶óÀÌÄÚ»çÀÌµå ¹× ¾Æ¸¶À̵å¿Í °°Àº È­ÇÕ¹°ÀÇ °¡¼öºÐÇØ¸¦ Ã˸ÅÇÏ´Â 6´ë È¿¼Ò±ºÀÇ ÀÏÁ¾.
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
GDP-mannose mannosyl hydrolase <enzyme> Hydrolyzes GDP-mannose or GDP-glucose to GDP and respective hexose; has little or no activity on other nucleotides, dinucleotides, nucleotide sugars or sugar phosphates; member of the mutt family; mw about 18 kD; genbank l11721
Registry number: EC 3.2.1.-
Synonym: e. Coli orf1.9 product, yefc gene product
(26 Jun 1999)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
GDPmannose 3,5-epimerase <enzyme> Reversible epimerises GDP-d-mannose to GDP-l-galactose
Registry number: EC 5.1.3.18
Synonym: GDPmannose epimerase
(26 Jun 1999)
GDPmannose dolicholphosphate mannosyltransferase <enzyme> Catalyses the formation of mannosylphosphodolichol from GDPmannose and dolichyl phosphate
Registry number: EC 2.4.1.83
Synonym: dolichol phosphate GDP mannose mannosyltransferase, dolichol phosphate mannose synthase, dolichyl mannosyl transferase, mdp synthase, mannosylphosphoryldolichol synthase, dolichyl phosphomannose synthase, dolichyl-p-mannose synthase, mannosylphosphodolichol synthase, mpd-synthase
(26 Jun 1999)
GDPmannose phosphorylase <enzyme> A transferase that catalyses the transfer of GDP to the mannose of mannose-1-phosphate.
Consider also the bifunctional enzyme, phosphomannose isomerase-guanosine diphospho-d-mannose pyrophosphorylase; rfbm has similarity to long-chain, iron-containing alcohol dehydrogenases
Registry number: EC 2.7.7.13
Synonym: GDPmannose phosphorylase, GDP mannose pyrophosphorylase, GTP-alpha-d-mannose-1-phosphate guanylyltransferase, GDP-mannose pyrophosphorylase, rfbm gene product, rfbm protein
(26 Jun 1999)
beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase <enzyme> Induced in preneoplastic stage of liver carcinogenesis promoted by orotic acid in rats; adds "bisecting n-acetylglucosaminyl residue in beta 1,4 linkage to the beta-linked mannose of the core of asparagine-linked oligosaccharides
Registry number: EC 2.4.1.144
Synonym: n-acetylglucosaminyltransferase III, udpgnac-glycopeptide beta4-n-acetylglucosaminyl transferase III, udpgnac-magtransferase III, udp-n-acetylglucosamine-beta-d-mannoside beta-1,4-n-acetylglucosaminyltransferase III
(26 Jun 1999)
mannosyl-glycoprotein endo-beta-n-acetylglucosaminidase <enzyme> A group of related enzymes responsible for the endohydrolysis of the di-n-acetylchitobiosyl unit in high-mannose-content glycopeptides and glycoproteins.
Chemical name: Glycopeptide-D-mannosyl-N(4)-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-beta-glucosaminohydrolase
Registry number: EC 3.2.1.96
(12 Dec 1998)
mannosyl-oligosaccharide 1,2-alpha-mannosidase <enzyme> Cleaves off terminal alpha-1,2-linked mannose residues resulting in the oligosaccharide man(9)glcnac(2)
Registry number: EC 3.2.1.113
Synonym: alpha-d-mannosidase I, mannosidase I, man9-mannosidase, man9-alpha-mannosidase, alpha 1,2-mannosidase, 1,2-alpha-d-mannosidase, msds protein
(26 Jun 1999)
mannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidase <enzyme> Removes alpha-1,3- and alpha-1,6-mannosyl residues during post-translational modification of glycoproteins; amino acid sequence of gmii (drosophila) given in second source; genbank x77652
Registry number: EC 3.2.1.114
Synonym: mannosidase II, alpha-d-mannosidase II, 1,3-(1,6-)mannosyl-oligosaccharide alpha-d-mannohydrolase, golgi alpha-mannosidase II, gmii gene product
(26 Jun 1999)
acetyl-CoA hydrolase <enzyme> An enzyme that catalyses reversibly the hydrolysis of acetyl-CoA to yield CoA and acetate. The enzyme is involved in the oxidation of fatty acids.
Chemical name: Acetyl-CoA hydrolase
Registry number: EC 3.1.2.1
(12 Dec 1998)
acyloxyacyl hydrolase <enzyme> Removes nonhydroxylated fatty acids from lipid a
Registry number: EC 3.1.1.-
(26 Jun 1999)
adenosine 5'-phosphoramidate hydrolase <enzyme> Hydrolyzes nucleoside 5'-monophosphoramidates into nucleoside 5'-phosphates and ammonia
Registry number: EC 3.9.1.-
Synonym: ampn hydrolase, nucleoside monophosphoramidate hydrolase
(26 Jun 1999)
ADP ribose-histone hydrolase <enzyme> Splits bond between ADP ribose and histone
Registry number: EC 4.2.99.-
Synonym: ADP-ribosyl histone splitting enzyme, ADP-ribosyl protein lyase
(26 Jun 1999)
ADPribosylarginine hydrolase <enzyme> Acts on adpribose arginine to yield adpribose and arginine
Registry number: EC 3.2.2.19
Synonym: adpribose-arginine cleavage enzyme, ADP-ra-cleavage enzyme, ADP-ribosylarginine hydrolase, ADP-ribosylarginine glycohydrolase, ADP-ribose-arginine cleavage enzyme, ADP-ribosylprotein hydrolase
(26 Jun 1999)
allophanate hydrolase <enzyme> An enzyme that catalyses the hydrolysis of allophanic acid to two molecules of ammonia plus two molecules of "active carbon dioxide".
Chemical name: Urea-1-carboxylate amidohydrolase
Registry number: EC 3.5.1.54
(12 Dec 1998)
alpha-hydroxymethyl-alpha'-(N-acetylaminomethylene)succinic acid hydrolase <enzyme> Involved in degradation of vitamin b6; forms acetic acid plus ammonia plus carbon dioxide plus alpha-hydroxymethyl-succinic monoaldehyde
Registry number: EC 3.5.1.-
Synonym: compound b hydrolase
(26 Jun 1999)
alpha-(N-acetylaminomethylene)succinic acid hydrolase <enzyme> Involved in degradation of vitamin b6; forms acetic acid plus ammonia plus carbon dioxide plus succinic monoaldehyde
Registry number: EC 3.5.1.-
Synonym: compound a hydrolase
(26 Jun 1999)
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
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °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 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °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
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °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