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「Ligase」の共起表現一覧(1語右で並び替え)

該当件数 : 48



discovered and first characterized E. coli DNA ligase, a key enzyme of genetic engineering and recom
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
acid synthetase, valine transfer ribonucleate ligase, and valine translase.
a-cholestanoyl coenzyme A synthetase, DHCA-CoA ligase, and 3alpha,7alpha-dihydroxy-5beta-cholestanat
number of other structures present in the DNA ligase are the AMP and lysine, both of which are impo
ames in common use include benzoate-coenzyme A ligase, benzoyl-coenzyme A synthetase, and benzoyl Co
biotin-[methylmalonyl-CoA-carboxyltransferase] ligase, biotin:apo[methylmalonyl-CoA:pyruvate carboxy
re initially charged with serine by seryl-tRNA ligase, but the resulting Ser-tRNA(Sec) is not used f
the ligation of restriction enzyme fragments, ligase can also join the ends on only one of the two
Glutamate cysteine ligase catalytic subunit (GCLC, ~73 kDa) possesses al
ther names in common use include citrate lyase ligase, citrate lyase synthetase, acetate: SH-acyl-ca
the Skp1/Cullin/F-box protein (SCF) ubiquitin ligase complex, which marks proteins for proteosomal
e pdb2ovq, which shows the SCF(Fbw7) ubiquitin ligase complex.
Instead, the mismatch sensitivity of a DNA ligase enzyme is used to determine the underlying seq
sozyme of the long-chain fatty-acid-coenzyme A ligase family.
by ligation relies upon the sensitivity of DNA ligase for base-pairing mismatches.
ne synthetase (EC 6.3.2.2) (glutamate cysteine ligase, GCL) is the first enzyme in the glutathione b
ynthetase, glutamine translase, glutamate-tRNA ligase, glutaminyl ribonucleic acid, and GlnRS.
n enzymology, an adenylyl-[glutamate---ammonia ligase] hydrolase (EC 3.1.4.15) is an enzyme that cat
of multiple DNA polymerases, DNA primase, DNA ligase I and is S phase-specific (since these enzymes
Vif hijacks the cellular Cullin5 E3 ubiquitin ligase in order to target APOBEC3G for degradation.
In enzymology, a phenylacetate-CoA ligase is an enzyme that catalyzes the chemical react
Glutamate cysteine ligase is a heterodimeric enzyme composed of two prot
The mechanism of DNA ligase is to form two covalent phosphodiester bonds b
DNA ligase is sensitive to the structure of DNA and has v
DNA ligase is an enzyme that joins together ends of DNA m
ansfer RNA synthetase, isoleucine-transfer RNA ligase, isoleucine-tRNA synthetase, and isoleucine tr
ves the primer, replacing it with DNA, and DNA ligase joins the ends to make another molecule of dou
t with KCNJ4, ID1, F11 receptor, SDC2, Parkin ( ligase), LIN7A, Nephrin, DLG4, RPH3A, DLG1, APBA1, KC
Glutamate cysteine ligase modifier subunit (GCLM, ~31 kDa) increases the
r names in common use include phenylacetyl-CoA ligase, PA-CoA ligase, and phenylacetyl-CoA ligase (A
include polyribonucleotide synthase (ATP), RNA ligase, polyribonucleotide ligase, and ribonucleic li
Some forms of DNA ligase present in bacteria (usually larger) may requi
ATP is required for the ligase reaction, which proceeds in three steps: (1) a
The RNA Ligase ribozyme was the first of several types of syn
Ligase ribozymes may have been part of such a pre-bio
Finally, DNA ligase seals the nicks to finish NER.
The APC is an E3 ubiquitin ligase that targets cell cycle regulatory proteins fo
virtue of highly discriminatory arginine-tRNA ligase, the enzyme responsible for the first step in
DNA ligase then forms a phosphodiester bond to seal the r
DNA sequencing method that uses the enzyme DNA ligase to identify the nucleotide present at a given
It can be used by DNA ligase to create overlapping "sticky ends" so that pr
hetase, D-glutamate-adding enzyme, D-glutamate ligase, UDP-Mur-NAC-L-Ala:D-Glu ligase, UDP-N-acetylm
ylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine, ligase, uridine diphosphoacetylmuramoylpentapeptide s
and by the enzyme formate-tetrahydrofolate ligase via the reaction
The first DNA ligase was purified and characterized in 1967.
encode the enzyme Phosphoribosylamine-glycine ligase, which catalyzes an early step in de novo puri
                                                                                                    


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