「COFACTOR」の共起表現(1語左で並び替え)

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共起表現

「COFACTOR」の共起表現一覧(1語左で並び替え)

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using NAD+ as a	cofactor.
It requires potassium as a	cofactor.
F2RL2 is a	cofactor for F2RL3 activation by thrombin.
thought to be a homodimer which uses FAD as a	cofactor.
ous enzyme which binds and requires NAD+ as a	cofactor.
An enzyme that uses adenosylcobalamin as a	cofactor is methylmalonyl-CoA mutase (MCM).
It acts mainly as a	cofactor on coagulation and inflammation, and has no i
Members of this family utilise FMN as a	cofactor and are often found to be homodimers.
se plasminogen activator receptor (uPAR) is a	cofactor for plasminogen activation by urokinase plasm
Fibrin is a	cofactor for plasminogen activation by tissue plasmino
An example of an enzyme that contains a	cofactor is carbonic anhydrase, and is shown in the ri
This reaction uses calcium as a	cofactor and plays an important role in the intracellu
meaning that it uses inorganic phosphate as a	cofactor to cleave nucleotide-nucleotide bonds, releas
4. acts as a	cofactor for phosphopentomutase, which produces D-ribo
A	cofactor is a non-protein chemical compound that is bo
complexed with a calcium ion and serves as a	cofactor in lactose synthesis, but has no tumoricidal
its, and its activity requires ascorbate as a	cofactor.
light, rhodopsin splits into a protein and a	cofactor: opsin and all-trans-retinal (a form of vitam
Its best known mechanism of action is as a	cofactor in the formation of coagulation factors II (p
This reaction uses calcium as a	cofactor and plays an important role in the intracellu
uses a covalently bound pyruvate residue as a	cofactor rather than the more common pyridoxal 5'-phos
in a reaction that requires vitamin B12 as a	cofactor.
oswitch that senses the presence of AdoCbl, a	cofactor needed for the breakdown of ethanolamine.
dary metabolite of white rot fungi, acts as a	cofactor for the enzyme
coagulation pathway, where it functions as a	cofactor to Protein C in the inactivation of Factors V
elated protein 5) is able to bind to act as a	cofactor for Factor I, has decay accelerating activity
II participates in blood coagulation; it is a	cofactor for factor IXa which, in the presence of Ca+2
activity-they usually require only Mg2+ as a	cofactor.
Particularly, it is an essential nutrient and	cofactor for the enzymatic synthesis of glutathione, a
l 3-phosphate dehydrogenase with NAD+/NADH as	cofactor.
tases including NADH dehydrogenase as well as	cofactor in biological blue-light photo receptors.
ng the configuration of a retinal Schiff base	cofactor inside the protein from the cis-form to the t
hat catalyze chemical reactions via the bound	cofactor flavin.
o auxilin, a neuronal cell uncoating clathrin	cofactor, in its amino acid composition.
e methyl coenzyme M reductase, which contains	cofactor F430 as the prosthetic group.
ther acids lower the pH and remove the copper	cofactor necessary for the responsible enzymes to func
d to chelate the prosthetic Cu(II)-bipyridine	cofactor complex in the enzyme lysyl oxidase.
tween the CYP domain and an electron donating	cofactor.
was discovered to play a role as an enzymatic	cofactor.
by a failure in the gene that makes an enzyme	cofactor for beta-hexosaminidase, called the GM2 activ
Zinc is an essential	cofactor for hundreds of enzymes.
Zinc is an essential	cofactor for more than 50 classes of enzymes.
erin (INN) is a naturally occurring essential	cofactor of the three aromatic amino acid hydroxylase
THB is an essential	cofactor required by the aromatic amino acid hydroxyla
n with two small molecules bound, for example	cofactor and substrate; or a complex formed between tw
onins are not thought to utilize a GroES-type	cofactor to fold their substrates.
Only the free form has	cofactor activity.
t (PsbE), one beta (PsbF) subunit, and a heme	cofactor.
Heparin	cofactor II, a protein encoded by the SERPIND1 gene, i
ions in this gene are associated with heparin	cofactor II deficiency.
Heparin	Cofactor II deficiency can lead to increased thrombin
tivities of both antithrombin III and heparin	cofactor II simultaneously.
tability of the TPP ring) and Glu-51 (aids in	cofactor binding).
lecular weights, and both require a metal ion	cofactor.
hich Hmd acts is unknown, the iron-containing	cofactor is in part responsible for the catalytic acti
plex contains the active factor IX (IXa), its	cofactor factor VIII (VIIIa), the substrate (factor X)
Aside from its	cofactor role for intracellular enzymes, FA also displ
e moiety is then transferred to the lipoamide	cofactor of the H protein.
em (including factor H, factor I and membrane	cofactor protein), with the factor H mutations being t
peptidases (EC 3.4.11.9) that utilize a metal	cofactor and remove the N-terminal amino acid from pep
ibes an atom as belonging to a small molecule	cofactor rather than to part of a biopolymer chain.
Molybdenum	cofactor is a cofactor required for the activity of en
Molybdenum	cofactor sulfurase is an enzyme that in humans is enco
Molybdenum	cofactor functions directly in ethylbenzene dehydrogen
MOCOS sulfurates the molybdenum	cofactor of xanthine dehydrogenase (XDH) and aldehyde
at the active site in a tricyclic molybdenum	cofactor.
d urine of babies can be caused by molybdenum	cofactor deficiency disease which leads to neurologica
Mo or W is inserted to give the molybdopterin	cofactor.
metallo-enzyme that utilizes a molybdopterin	cofactor and a heme group.
contain a selenide-ligand to a molybdopterin	cofactor at their active sites (e.g.
of sulfite oxidase contains the molybdopterin	cofactor and supports molybdenum in its highest oxidat
the concomitant oxidation of a NADH or NADPH	cofactor.
Using an NADPH	cofactor and FAD prosthetic group, these microsomal pr
nteresting because OMP decarboxylases uses no	cofactor and contains no metal sites or prosthetic gro
of B12 is insufficient for the conversion of	cofactor methylmalonyl-CoA into succinyl-CoA, the buil
It employs one	cofactor, FAD.
It employs one	cofactor, heme.
It employs one	cofactor, copper.
It employs one	cofactor, cobamide.
It employs one	cofactor, flavoprotein.
It employs one	cofactor, zinc.
It employs one	cofactor, iron.
It employs one	cofactor, FMN.
It employs one	cofactor, manganese.
It employs one	cofactor, ATP.
It employs one	cofactor, calcium.
It employs one	cofactor, metal.
It employs one	cofactor, NAD+.
It employs one	cofactor, adenosylcobalamin.
It employs one	cofactor, PQQ.
It employs one	cofactor, ferredoxin.
It employs one	cofactor, cadmium.
It employs one	cofactor, ADP.
It employs one	cofactor, magnesium.
It has one	cofactor, FAD.
It employs one	cofactor, cobalt.
It employs one	cofactor, biotin.
It employs one	cofactor, molybdenum.
It employs one	cofactor, thiamin diphosphate.
It employs one	cofactor, pyridoxal phosphate.
This enzyme employs one	cofactor, iron.
It employs one	cofactor, neutral salt.
It employs one	cofactor, nicotinamide D-ribonucleotide.
It employs one	cofactor, iron-sulfur.
It has one	cofactor: the flavin FAD.
It employs one	cofactor, heme-thiolate(P-450).
of two enzymes sharing a single substrate or	cofactor, also referred to as a biochemical switching
The first organic	cofactor to be discovered was NAD+, which was identifi
nase from E. coli with Pyridoxal 5' Phosphate	cofactor
up of glycine through its pyridoxal phosphate	cofactor.
aldehydes, especially the pyridoxal phosphate	cofactor of many Vitamin B6-dependent enzymes.
Factor I requires a C3b-binding protein	cofactor such as complement factor H, CR1 and Membrane
e serine protease, Factor Xa, and the protein	cofactor, Factor Va.
aredoxin, a 2Fe-2S cluster-containing protein	cofactor.
s discovered by J.G. Hauge as the third redox	cofactor after nicotinamide and flavin in bacteria (al
h PDLIM1, Sodium-hydrogen exchange regulatory	cofactor 2, Collagen, type XVII, alpha 1, CAMK2A, CAMK
Sodium-hydrogen exchange regulatory	cofactor 2 has been shown to interact with SGK, Actini
Sodium-hydrogen exchange regulatory	cofactor NHE-RF2 (NHERF-2) also known as tyrosine kina
S-adenosyl-L-methionine ('SAM') is a required	cofactor.
It is restored to the required	cofactor tetrahydrobiopterin by dihydrobiopterin reduc
A negative Shannon	cofactor is the same, but sets all x's to 0.
A positive Shannon	cofactor of function F with respect to variable x is d
in the Vmax or Km for the tetrahydrobiopterin	cofactor.
suppose we wish to find the	cofactor C23.
Specifically the	cofactor of the (i, j) entry of a matrix, also known a
notably in the amino acid methionine and the	cofactor biotin.
(coupled to ADP) in a step that activates the	cofactor toward binding Mo or W.
The	cofactor Mg2+ is believed to bind water molecules and
In linear algebra, the	cofactor (sometimes called adjunct, see ) describes a
ed mutations that experimentally switched the	cofactor specificity of Candida boidinii xylose reduct
Type II restriction enzymes, but require the	cofactor AdoMet to be active.
ls if the protein cannot effectively bind the	cofactor NAD+, as shown in the G16S mutation.
s a Rossman fold and interactions between the	cofactor and the fold allow for the isomerization of t
cerol monooxygenase critically depends on the	cofactor tetrahydrobiopterin and iron.
fI cleavage substrates (C3b and C4b) and the	cofactor proteins needed for cleavage of C3b (Factor H
enzymes so far identified in nature use this	cofactor, save for the phylogenetically ancient molybd
xidoreductase (AOR) family contain a tungsten	cofactor and an 4Fe4S cluster.
ging concentrations of molybdenum or tungsten	cofactor .

共起表現

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