¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"carboxylase"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
À̰ÍÀ» ¿øÇϼ̽À´Ï±î?
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • carboxylase
    Ä«¸£º¹½Ç¶ó¾ÆÁ¦
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • carboxylase
    Ä«¸£º¹½Ç¶ó¾ÆÁ¦
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • carboxylase
    Ä«¸£º¹½Ç¶ó¾ÆÁ¦.
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 8 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • acetyl coenzyme A carboxylase
    ¾Æ¼¼Æ¿º¸È¿¼Ò(ÜÍý£áÈ)A Ä«¸£º¹½Ç·¹À̽º
  • biotin carboxylase
    ¹ÙÀÌ¿Àƾ Ä«¸£º¹½Ç·¹À̽º
  • diphosphoribulose carboxylase
    "ÀÌÀλê(ì£×òß«)¶óÀ̺ҷνº Ä«¸£º¹½Ç·¹À̽º, (ÔÒ) ribulose-I, 5-bisphosphate carboxylase"
  • pentose phosphate carboxylase
    Àλê(×òß«)ÆæÅ佺 Ä«¸£º¹½Ç·¹À̽º
  • phosphoenolpyruvate carboxylase
    Æ÷½ºÆ÷¿¡³îÆÄÀÌ·çºê»ê(ß«) Ä«¸£º¹½Ç·¹À̽º
  • pyruvate carboxylase
    ÆÄÀÌ·çºê»ê(ß«) Ä«¸£º¹½Ç·¹À̽º
  • "ribulose-1,5-bisphosphate carboxylase"
    "¶óÀ̺ҷνº 1,5 ¾çÀλê(å»×òß«)Ä«¸£º¹½Ç·¹À̽º"
  • RuBP carboxylase
    RuBP Ä«¸£º¹½Ç¶óÁ¦
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
DDC L-Dopa De-Carboxylase
PC   1) Phosphatidyl Choline
  2) Pyruvate Carboxylase
ACC accommodation; acetyl coenzyme A carboxylase; acinic cell carcinoma; acute care center; adenoid cyst...
BMCC beta-methylcrotonyl coenzyme A carboxylase
GGC gamma-glutamyl carboxylase
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
ACC Acetyl coenzyme A carboxylase
ACC Acetyl-CoA carboxylase
ACCase Acetyl-CoA carboxylase
RuBisCO D-ribulose-1,5-bisphosphate carboxylase/oxygenase
PEPC phosphoeno/pyruvate carboxylase
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • carboxylase
    Ä«¸£º¹½Ç¶ó¾ÆÁ¦
    ¾ËÆÄ ŰÅä»êÀÇ Ä«¸£º¹½Ç±â¿¡¼­ ÀÌ»êÈ­ ź¼Ò¸¦ Á¦°ÅÇÏ´Â È¿¼Ò. ÆÄÀÌ·çºó»êÀÇ Å»Åº»êÀº ¾ËÄÝ ¹ßÈ¿¿¡¼­ Áß¿äÇÑ ´Ü°è·Î¼­, ÆÄÀÌ·çºó»êÀÌ ¾Æ¼¼Æ®¾Ëµ¥ÇÏÀ̵å¿Í ÀÌ»êÈ­ ź¼Ò·Î ÀüȯÇÑ´Ù.
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
carboxylase 1. One of several carboxy-lyases, trivially named carboxylases or decarboxylases (EC subclass 4.1.1), catalyzing the addition of CO2 to all or part of another molecule to create an additional -COOH group (e.g., ribulose-1,5-bisphosphate carboxylase).
2. Obsolete name for pyruvate decarboxylase.
(05 Mar 2000)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
acetone carboxylase <enzyme> An ATP-dependent carboxylase
Registry number: EC 4.1.1.-
(26 Jun 1999)
acetyl-CoA carboxylase <enzyme> A carboxylating enzyme that catalyses the conversion of ATP, acetyl-CoA, and hco3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyses transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA
Chemical name: Acetyl-CoA:carbon-dioxide ligase (ADP-forming)
Registry number: EC 6.4.1.2
(12 Dec 1998)
acetyl CoA carboxylase phosphatase <enzyme> Phosphatase occurs in complex with the carboxylase
Registry number: EC 3.1.3.-
Synonym: acc-phosphatase, acetyl coenzyme a carboxylase phosphatase
(26 Jun 1999)
acyl-CoA carboxylase <enzyme> Catalyses carboxylation (ATP, mg ++, mco(3)-dependent) of acetyl-CoA, propionyl CoA, and butyryl CoA; from nematode turbatrix aceti
Registry number: EC 6.4.1.-
Synonym: acyl-coenzyme a carboxylase
(26 Jun 1999)
biotin carboxylase <enzyme> A subunit of acetyl-CoA carboxylase
Registry number: EC 6.3.4.14
(26 Jun 1999)
gamma-glutamyl carboxylase <enzyme> An enzyme that catalyses the formation of gamma-carboxyglutamyl residues in many proteins, several appearing in the blood clotting cascade.
(05 Mar 2000)
glutamyl carboxylase <enzyme> Carboxylates glutamyl residues in a microsomal protein precursor of plasma prothrombin to form gamma-carboxyglutamic acid residues
Registry number: EC 6.4.-
Synonym: vitamin k-dependent carboxylase, glutamate carboxylase, vitamin k dependent carboxylase, vitamin k-dependent gamma-glutamyl carboxylase, k-dependent carboxylase, gamma-glutamyl carboxylase
(26 Jun 1999)
PEP carboxylase <enzyme> Enzyme responsible for the primary fixation of carbon dioxide in C4 plants. Carboxylates PEP phosphoenolpyruvate to give oxaloacetate. Also important in crassulacean acid metabolism, since it is responsible for carbon dioxide fixation in the dark.
(18 Nov 1997)
ribulose-1,5-bisphosphate carboxylase A dimerizing carboxy-lyase; an enzyme that catalyses the addition of carbon dioxide to d-ribulose 1,5-bisphosphate and the hydrolysis of the addition product to two molecules of 3-d-phosphoglyceric acid, a key reaction in the fixation of CO2 in photosynthesis.
Synonym: carboxydismutase.
(05 Mar 2000)
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)
ribulose bisphosphate carboxylase <enzyme> A copper protein that catalyses the formation of 2 moles of 3-phosphoglycerate from ribulose 1,5-biphosphate in the presence of carbon dioxide and is responsible for carbon dioxide fixation in photosynthesis.
Carbon dioxide is combined with ribulose diphosphate to give two molecules of 3 phosphoglycerate, as part of the Calvin Benson cycle. It is the sole carbon dioxide fixing enzyme in C3 plants and collaborates with PEP carboxylase in carbon dioxide fixation in C4 plants.
In the presence of oxygen the products of the reaction are one molecule of phosphoglyceric acid and one molecule of phosphoglycolic acid. The latter is the initial substrate for photorespiration and this oxygenase function occurs in C3 plants where the enzyme is not protected from ambient oxygen, in C4 plants the enzyme acts exclusively as a carboxylase since it is protected from oxygen.
Also called Fraction 1 protein, the major protein of leaves.
Chemical name: 3-Phospho-D-glycerate carboxy-lyase (dimerizing)
Registry number: EC 4.1.1.39
(12 Dec 1998)
ribulosebisphosphate carboxylase-oxygenase activase <chemical> Requires ATP; amino acid sequence given in first source
Synonym: rubisco activase, rca protein
(26 Jun 1999)
ribulose diphosphate carboxylase <enzyme> A copper protein that catalyses the formation of 2 moles of 3-phosphoglycerate from ribulose 1,5-biphosphate in the presence of carbon dioxide and is responsible for carbon dioxide fixation in photosynthesis.
Carbon dioxide is combined with ribulose diphosphate to give two molecules of 3 phosphoglycerate, as part of the Calvin Benson cycle. It is the sole carbon dioxide fixing enzyme in C3 plants and collaborates with PEP carboxylase in carbon dioxide fixation in C4 plants.
In the presence of oxygen the products of the reaction are one molecule of phosphoglyceric acid and one molecule of phosphoglycolic acid. The latter is the initial substrate for photorespiration and this oxygenase function occurs in C3 plants where the enzyme is not protected from ambient oxygen, in C4 plants the enzyme acts exclusively as a carboxylase since it is protected from oxygen.
Also called Fraction 1 protein, the major protein of leaves.
Chemical name: 3-Phospho-D-glycerate carboxy-lyase (dimerizing)
Registry number: EC 4.1.1.39
(12 Dec 1998)
RuDP carboxylase <enzyme> A copper protein that catalyses the formation of 2 moles of 3-phosphoglycerate from ribulose 1,5-biphosphate in the presence of carbon dioxide and is responsible for carbon dioxide fixation in photosynthesis.
Carbon dioxide is combined with ribulose diphosphate to give two molecules of 3 phosphoglycerate, as part of the Calvin Benson cycle. It is the sole carbon dioxide fixing enzyme in C3 plants and collaborates with PEP carboxylase in carbon dioxide fixation in C4 plants.
In the presence of oxygen the products of the reaction are one molecule of phosphoglyceric acid and one molecule of phosphoglycolic acid. The latter is the initial substrate for photorespiration and this oxygenase function occurs in C3 plants where the enzyme is not protected from ambient oxygen, in C4 plants the enzyme acts exclusively as a carboxylase since it is protected from oxygen.
Also called Fraction 1 protein, the major protein of leaves.
Chemical name: 3-Phospho-D-glycerate carboxy-lyase (dimerizing)
Registry number: EC 4.1.1.39
(12 Dec 1998)
phosphoenolpyruvate carboxylase <enzyme> An enzyme with high affinity for carbon dioxide. It catalyses irreversibly the formation of oxaloacetate from phosphoenolpyruvate and carbon dioxide. This fixation of carbon dioxide in several bacteria and some plants is the first step in the biosynthesis of glucose.
Chemical name: Orthophosphate:oxaloacetate carboxy-lyase (phosphorylating)
Registry number: EC 4.1.1.31
(12 Dec 1998)
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 2 ÆäÀÌÁö: 1
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
carboxylase an enzyme that catalyzes the addition of a molecule of carbon dioxide to another compound to form a carboxyl group. The carboxylases include some carboxy-lyases [EC 4.1.1] and those ligases, usually biotinyl-proteins, that cleave ATP to drive the reaction [EC 6.4.1].
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 4 ÆäÀÌÁö: 1
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 À¯»ç °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 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 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °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 À¯»ç °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 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 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 À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 1
ÅëÇÕ°Ë»ö ¿Ï·á