「Ligase」の共起表現一覧(1語左で並び替え)
該当件数 : 172件
sozyme of the long-chain fatty-acid-coenzyme A | ligase family. |
ames in common use include benzoate-coenzyme A | ligase, benzoyl-coenzyme A synthetase, and benzoyl Co |
e-CoA synthetase, 4-hydroxybenzoate-coenzyme A | ligase (AMP-forming), 4-hydroxybenzoyl coenzyme A syn |
In enzymology, an acetate-CoA | ligase (ADP-forming) (EC 6.2.1.13) |
matic name of this enzyme class is acetate:CoA | ligase (ADP-forming). |
In enzymology, an acetoacetate-CoA | ligase (EC 6.2.1.16) |
name of this enzyme class is acetoacetate:CoA | ligase (AMP-forming). |
of this enzyme class is acetone:carbon-dioxide | ligase (AMP-forming). |
this enzyme class is L-amino acid:L-amino acid | ligase (ADP-forming). |
, bacilysin synthetase, YwfE, and L-amino acid | ligase. |
In enzymology, an acid-CoA | ligase (GDP-forming) (EC 6.2.1.10) |
stematic name of this enzyme class is acid:CoA | ligase (GDP-forming). |
n enzymology, an adenylyl-[glutamate---ammonia | ligase] hydrolase (EC 3.1.4.15) is an enzyme that cat |
enzyme class is adenylyl-[L-glutamate:ammonia | ligase (ADP-forming)] adenylylhydrolase. |
e MurE synthetase [ambiguous], alanine:alanine | ligase (ADP-forming), and alanylalanine synthetase. |
this enzyme class is alpha-tubulin:L-tyrosine | ligase (ADP-forming). |
In enzymology, an arachidonate-CoA | ligase (EC 6.2.1.15) |
name of this enzyme class is arachidonate:CoA | ligase (AMP-forming). |
virtue of highly discriminatory arginine-tRNA | ligase, the enzyme responsible for the first step in |
In enzymology, an aspartate-ammonia | ligase (ADP-forming) (EC 6.3.1.4) |
In enzymology, an aspartate-ammonia | ligase (EC 6.3.1.1) |
In enzymology, an aspartate-tRNA | ligase (EC 6.1.1.12) |
In enzymology, an aspartate-tRNAAsn | ligase (EC 6.1.1.23) |
this enzyme class is ATP:[L-glutamate:ammonia | ligase (ADP-forming)] adenylyltransferase. |
In enzymology, a benzoate-CoA | ligase (EC 6.2.1.25) |
atic name of this enzyme class is benzoate:CoA | ligase (AMP-forming). |
biotin-carboxyl-carrier-protein:carbon-dioxide | ligase (ADP-forming). |
In enzymology, a biotin-CoA | ligase (EC 6.2.1.11) |
gy, a biotin-[methylcrotonoyl-CoA-carboxylase] | ligase (EC 6.3.4.11) is an enzyme that catalyzes the |
biotin-[methylmalonyl-CoA-carboxyltransferase] | ligase, biotin:apo[methylmalonyl-CoA:pyruvate carboxy |
biotin-[methylmalonyl-CoA-carboxytransferase] | ligase (EC 6.3.4.9) is an enzyme that catalyzes the c |
otin:apo-[3-methylcrotonoyl-CoA:carbon-dioxide | ligase (ADP-forming)] ligase (AMP-forming). |
ss is biotin:apo-[propanoyl-CoA:carbon-dioxide | ligase (ADP-forming)] ligase (AMP-forming). |
ematic name of this enzyme class is biotin:CoA | ligase (AMP-forming). |
methylmalonyl-CoA:pyruvate carboxytransferase] | ligase (AMP-forming). |
Glutamate cysteine | ligase is a heterodimeric enzyme composed of two prot |
Glutamate cysteine | ligase modifier subunit (GCLM, ~31 kDa) increases the |
Glutamate cysteine | ligase catalytic subunit (GCLC, ~73 kDa) possesses al |
ne synthetase (EC 6.3.2.2) (glutamate cysteine | ligase, GCL) is the first enzyme in the glutathione b |
In enzymology, a cysteine-tRNA | ligase (EC 6.1.1.16) |
In enzymology, a D-alanine-D-alanine | ligase (EC 6.3.2.4) is an enzyme that catalyzes the c |
me of this enzyme class is D-alanine:D-alanine | ligase (ADP-forming). |
hetase, D-glutamate-adding enzyme, D-glutamate | ligase, UDP-Mur-NAC-L-Ala:D-Glu ligase, UDP-N-acetylm |
activating enzyme, and D-pantoate:beta-alanine | ligase (AMP-forming). |
a-cholestanoyl coenzyme A synthetase, DHCA-CoA | ligase, and 3alpha,7alpha-dihydroxy-5beta-cholestanat |
In enzymology, a dicarboxylate-CoA | ligase (EC 6.2.1.23) |
In enzymology, a diphthine-ammonia | ligase (EC 6.3.2.22) is an enzyme that catalyzes the |
name of this enzyme class is diphthine:ammonia | ligase (ADP-forming). |
discovered and first characterized E. coli DNA | ligase, a key enzyme of genetic engineering and recom |
The mechanism of DNA | ligase is to form two covalent phosphodiester bonds b |
DNA sequencing method that uses the enzyme DNA | ligase to identify the nucleotide present at a given |
Instead, the mismatch sensitivity of a DNA | ligase enzyme is used to determine the underlying seq |
DNA | ligase is sensitive to the structure of DNA and has v |
of multiple DNA polymerases, DNA primase, DNA | ligase I and is S phase-specific (since these enzymes |
e last phosphodiester bond is completed by DNA | ligase. |
It can be used by DNA | ligase to create overlapping "sticky ends" so that pr |
ves the primer, replacing it with DNA, and DNA | ligase joins the ends to make another molecule of dou |
DNA | ligase then forms a phosphodiester bond to seal the r |
Some forms of DNA | ligase present in bacteria (usually larger) may requi |
number of other structures present in the DNA | ligase are the AMP and lysine, both of which are impo |
The first DNA | ligase was purified and characterized in 1967. |
Finally, DNA | ligase seals the nicks to finish NER. |
DNA | ligase is an enzyme that joins together ends of DNA m |
by ligation relies upon the sensitivity of DNA | ligase for base-pairing mismatches. |
and by the enzyme formate-tetrahydrofolate | ligase via the reaction |
In enzymology, a formate-tetrahydrofolate | ligase (EC 6.3.4.3) is an enzyme that catalyzes the c |
the ligation of restriction enzyme fragments, | ligase can also join the ends on only one of the two |
ss is gamma-L-glutamyl-L-cysteine:beta-alanine | ligase (ADP-forming). |
e class is gamma-L-glutamyl-L-cysteine:glycine | ligase (ADP-forming). |
amma-L-glutamyl-L-cysteinyl-glycine:spermidine | ligase (ADP-forming) [spermidine is numbered so that |
is enzyme class is geranoyl-CoA:carbon-dioxide | ligase (ADP-forming). |
In enzymology, a glutamate-ethylamine | ligase (EC 6.3.1.6) |
In enzymology, a glutamate-putrescine | ligase (EC 6.3.1.11) |
ynthetase, glutamine translase, glutamate-tRNA | ligase, glutaminyl ribonucleic acid, and GlnRS. |
In enzymology, a glutamate-tRNA | ligase (EC 6.1.1.17) |
In enzymology, a glutamate-tRNAGln | ligase (EC 6.1.1.24) |
In enzymology, a glutamine-tRNA | ligase (EC 6.1.1.18) |
In enzymology, a glutarate-CoA | ligase (EC 6.2.1.6) |
tic name of this enzyme class is glutarate:CoA | ligase (ADP-forming). |
s enzyme is also called glutathione:spermidine | ligase (ADP-forming). |
In enzymology, a glycine-tRNA | ligase (EC 6.1.1.14) |
c name of this enzyme class is glycine:tRNAGly | ligase (AMP-forming). |
In enzymology, a histidine-tRNA | ligase (EC 6.1.1.21) |
In enzymology, an isoleucine-tRNA | ligase (EC 6.1.1.5) |
me of this enzyme class is L-aspartate:ammonia | ligase (ADP-forming). |
me of this enzyme class is L-aspartate:ammonia | ligase (AMP-forming). |
me of this enzyme class is L-aspartate:tRNAAsp | ligase (AMP-forming). |
me of this enzyme class is L-aspartate:tRNAAsx | ligase (AMP-forming). |
ame of this enzyme class is L-cysteine:tRNACys | ligase (AMP-forming). |
of this enzyme are ATP and L-glutamate:ammonia | ligase (ADP-forming), whereas its two products are di |
of this enzyme class is L-glutamate:ethylamine | ligase (ADP-forming). |
of this enzyme class is L-glutamate:putrescine | ligase (ADP-forming). |
me of this enzyme class is L-glutamate:tRNAGlu | ligase (AMP-forming). |
me of this enzyme class is L-glutamate:tRNAGlx | ligase (AMP-forming). |
me of this enzyme class is L-glutamine:tRNAGln | ligase (AMP-forming). |
this enzyme class is L-histidine:beta-alanine | ligase (AMP-forming). |
me of this enzyme class is L-histidine:tRNAHis | ligase (AMP-forming). |
e of this enzyme class is L-isoleucine:tRNAIle | ligase (AMP-forming). |
name of this enzyme class is L-leucine:tRNALeu | ligase (AMP-forming). |
name of this enzyme class is L-lysine:tRNAPyl | ligase (AMP-forming). |
e of this enzyme class is L-methionine:tRNAMet | ligase (AMP-forming). |
name of this enzyme class is L-proline:tRNAPro | ligase (AMP-forming). |
name of this enzyme class is L-serine:tRNASer | ligase (AMP-forming). |
me of this enzyme class is L-threonine:tRNAThr | ligase (AMP-forming). |
tophanyl-tRNA synthetase, L-tryptophan-tRNATrp | ligase (AMP-forming), tryptophanyl-transfer ribonucle |
e of this enzyme class is L-tryptophan:tRNATrp | ligase (AMP-forming). |
of this enzyme class is L-tyrosine:L-arginine | ligase (AMP-forming). |
ame of this enzyme class is L-tyrosine:tRNATyr | ligase (AMP-forming). |
name of this enzyme class is L-valine:tRNAVal | ligase (AMP-forming). |
In enzymology, a leucine-tRNA | ligase (EC 6.1.1.4) |
Long-chain-fatty-acid-CoA | ligase 4 is an enzyme that in humans is encoded by th |
Long-chain-fatty-acid-CoA | ligase 3 is an enzyme that in humans is encoded by th |
Long-chain-fatty-acid-CoA | ligase ACSBG1 is an enzyme that in humans is encoded |
Long-chain-fatty-acid-CoA | ligase ACSBG2 is an enzyme that in humans is encoded |
Long-chain-fatty-acid-CoA | ligase 5 is an enzyme that in humans is encoded by th |
Long-chain-fatty-acid-CoA | ligase 1 is an enzyme that in humans is encoded by th |
y, a long-chain-fatty-acid-luciferin-component | ligase (EC 6.2.1.19) |
a long-chain-fatty-acid-[acyl-carrier-protein] | ligase (EC 6.2.1.20) |
enzyme class is long-chain-fatty-acid:protein | ligase (AMP-forming). |
s long-chain-fatty-acid:[acyl-carrier-protein] | ligase (AMP-forming). |
ther names in common use include citrate lyase | ligase, citrate lyase synthetase, acetate: SH-acyl-ca |
In enzymology, a lysine-tRNAPyl | ligase (EC 6.1.1.25) |
In enzymology, a methionine-tRNA | ligase (EC 6.1.1.10) |
In mammals, there are four specific types of | ligase. |
f this enzyme class is omega-dicarboxylate:CoA | ligase (AMP-forming). |
In enzymology, an oxalate-CoA | ligase (EC 6.2.1.8) |
matic name of this enzyme class is oxalate:CoA | ligase (AMP-forming). |
In enzymology, a pantoate-beta-alanine | ligase (EC 6.3.2.1) is an enzyme that catalyzes the c |
t with KCNJ4, ID1, F11 receptor, SDC2, Parkin ( | ligase), LIN7A, Nephrin, DLG4, RPH3A, DLG1, APBA1, KC |
Parkin ( | ligase), |
In enzymology, a phenylacetate-CoA | ligase is an enzyme that catalyzes the chemical react |
name of this enzyme class is phenylacetate:CoA | ligase (AMP-forming). |
r names in common use include phenylacetyl-CoA | ligase, PA-CoA ligase, and phenylacetyl-CoA ligase (A |
encode the enzyme Phosphoribosylamine-glycine | ligase, which catalyzes an early step in de novo puri |
In enzymology, a phytanate-CoA | ligase (EC 6.2.1.24) |
tic name of this enzyme class is phytanate:CoA | ligase (AMP-forming). |
This enzyme is also called phytanoyl-CoA | ligase. |
s is poly(ribonucleotide):poly(ribonucleotide) | ligase (AMP-forming). |
In enzymology, a proline-tRNA | ligase (EC 6.1.1.15) |
se, prolyl-s-RNA synthetase, and prolinyl-tRNA | ligase. |
acid synthetase, valine transfer ribonucleate | ligase, and valine translase. |
The RNA | Ligase ribozyme was the first of several types of syn |
ansfer RNA synthetase, isoleucine-transfer RNA | ligase, isoleucine-tRNA synthetase, and isoleucine tr |
include polyribonucleotide synthase (ATP), RNA | ligase, polyribonucleotide ligase, and ribonucleic li |
In enzymology, an RNA | ligase (ATP) (EC 6.5.1.3) |
In enzymology, a serine-tRNA | ligase (EC 6.1.1.11) |
re initially charged with serine by seryl-tRNA | ligase, but the resulting Ser-tRNA(Sec) is not used f |
In enzymology, a succinate-CoA | ligase (ADP-forming) (EC 6.2.1.5) |
tic name of this enzyme class is succinate:CoA | ligase (ADP-forming). |
ATP is required for the | ligase reaction, which proceeds in three steps: (1) a |
In enzymology, a threonine-tRNA | ligase (EC 6.1.1.3) |
e of this enzyme class is trans-ferulate:CoASH | ligase (ATP-hydrolysing). |
In enzymology, a tryptophan-tRNA | ligase (EC 6.1.1.2) is an enzyme that catalyzes the c |
In enzymology, a tubulin-tyrosine | ligase (EC 6.3.2.25) is an enzyme that catalyzes the |
In enzymology, a tyrosine-arginine | ligase (EC 6.3.2.24) is an enzyme that catalyzes the |
In enzymology, a tyrosine-tRNA | ligase (EC 6.1.1.1) |
e pdb2ovq, which shows the SCF(Fbw7) ubiquitin | ligase complex. |
endent degradation by SCFGrrl, an E3 ubiquitin | ligase. |
and substrate specificity of this E3 ubiquitin | ligase. |
The APC is an E3 ubiquitin | ligase that targets cell cycle regulatory proteins fo |
the Skp1/Cullin/F-box protein (SCF) ubiquitin | ligase complex, which marks proteins for proteosomal |
Vif hijacks the cellular Cullin5 E3 ubiquitin | ligase in order to target APOBEC3G for degradation. |
an UDP-N-acetylmuramoyl-L-alanine-D-glutamate | ligase (EC 6.3.2.9) is an enzyme that catalyzes the c |
is UDP-N-acetylmuramoyl-L-alanine:D-glutamate | ligase (ADP-forming). |
-alanyl-D-glutamyl-L-lysine:D-alanyl-D-alanine | ligase (ADP-forming). |
N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine | ligase (EC 6.3.2.10) is an enzyme that catalyzes the |
ylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine, | ligase, uridine diphosphoacetylmuramoylpentapeptide s |
In enzymology, a valine-tRNA | ligase (EC 6.1.1.9) |
'synthetase' is to be used synonymously with ' | ligase'. |
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