「cofactor」の共起表現(1語右で並び替え)

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「cofactor」の共起表現一覧(1語右で並び替え)

cofactor

1語右で並び替え

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Only the free form has cofactor activity.
It employs one cofactor, adenosylcobalamin.
Type II restriction enzymes, but require the cofactor AdoMet to be active.
It employs one cofactor, ADP.
s discovered by J.G. Hauge as the third redox cofactor after nicotinamide and flavin in bacteria (al
of two enzymes sharing a single substrate or cofactor, also referred to as a biochemical switching
xidoreductase (AOR) family contain a tungsten cofactor and an 4Fe4S cluster.
Members of this family utilise FMN as a cofactor and are often found to be homodimers.
metallo-enzyme that utilizes a molybdopterin cofactor and a heme group.
This reaction uses calcium as a cofactor and plays an important role in the intracellu
of sulfite oxidase contains the molybdopterin cofactor and supports molybdenum in its highest oxidat
nteresting because OMP decarboxylases uses no cofactor and contains no metal sites or prosthetic gro
This reaction uses calcium as a cofactor and plays an important role in the intracellu
s a Rossman fold and interactions between the cofactor and the fold allow for the isomerization of t
peptidases (EC 3.4.11.9) that utilize a metal cofactor and remove the N-terminal amino acid from pep
n with two small molecules bound, for example cofactor and substrate; or a complex formed between tw
Using an NADPH cofactor and FAD prosthetic group, these microsomal pr
contain a selenide-ligand to a molybdopterin cofactor at their active sites (e.g.
It employs one cofactor, ATP.
tability of the TPP ring) and Glu-51 (aids in cofactor binding).
It employs one cofactor, biotin.
notably in the amino acid methionine and the cofactor biotin.
suppose we wish to find the cofactor C23.
It employs one cofactor, cadmium.
It employs one cofactor, calcium.
It employs one cofactor, cobalt.
It employs one cofactor, cobamide.
d to chelate the prosthetic Cu(II)-bipyridine cofactor complex in the enzyme lysyl oxidase.
It employs one cofactor, copper.
d urine of babies can be caused by molybdenum cofactor deficiency disease which leads to neurologica
e methyl coenzyme M reductase, which contains cofactor F430 as the prosthetic group.
e serine protease, Factor Xa, and the protein cofactor, Factor Va.
plex contains the active factor IX (IXa), its cofactor factor VIII (VIIIa), the substrate (factor X)
It employs one cofactor, FAD.
It has one cofactor, FAD.
It employs one cofactor, ferredoxin.
hat catalyze chemical reactions via the bound cofactor flavin.
It employs one cofactor, flavoprotein.
It employs one cofactor, FMN.
Zinc is an essential cofactor for hundreds of enzymes.
F2RL2 is a cofactor for F2RL3 activation by thrombin.
Zinc is an essential cofactor for more than 50 classes of enzymes.
se plasminogen activator receptor (uPAR) is a cofactor for plasminogen activation by urokinase plasm
Fibrin is a cofactor for plasminogen activation by tissue plasmino
Particularly, it is an essential nutrient and cofactor for the enzymatic synthesis of glutathione, a
by a failure in the gene that makes an enzyme cofactor for beta-hexosaminidase, called the GM2 activ
4. acts as a cofactor for phosphopentomutase, which produces D-ribo
dary metabolite of white rot fungi, acts as a cofactor for the enzyme
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
Molybdenum cofactor functions directly in ethylbenzene dehydrogen
It employs one cofactor, heme-thiolate(P-450).
It employs one cofactor, heme.
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.
Heparin cofactor II, a protein encoded by the SERPIND1 gene, i
complexed with a calcium ion and serves as a cofactor in lactose synthesis, but has no tumoricidal
o auxilin, a neuronal cell uncoating clathrin cofactor, in its amino acid composition.
Its best known mechanism of action is as a cofactor in the formation of coagulation factors II (p
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
It employs one cofactor, iron-sulfur.
It employs one cofactor, iron.
This enzyme employs one cofactor, iron.
Molybdenum cofactor is a cofactor required for the activity of en
A negative Shannon cofactor is the same, but sets all x's to 0.
An enzyme that uses adenosylcobalamin as a cofactor is methylmalonyl-CoA mutase (MCM).
An example of an enzyme that contains a cofactor is carbonic anhydrase, and is shown in the ri
A cofactor is a non-protein chemical compound that is bo
hich Hmd acts is unknown, the iron-containing cofactor is in part responsible for the catalytic acti
The pyridoxal 5'-phosphate (PLP) cofactor lies in and above the mouth of the alpha/beta
It employs one cofactor, magnesium.
It employs one cofactor, manganese.
It employs one cofactor, metal.
of B12 is insufficient for the conversion of cofactor methylmalonyl-CoA into succinyl-CoA, the buil
The cofactor Mg2+ is believed to bind water molecules and
It employs one cofactor, molybdenum.
ls if the protein cannot effectively bind the cofactor NAD+, as shown in the G16S mutation.
It employs one cofactor, NAD+.
ther acids lower the pH and remove the copper cofactor necessary for the responsible enzymes to func
oswitch that senses the presence of AdoCbl, a cofactor needed for the breakdown of ethanolamine.
It employs one cofactor, neutral salt.
Sodium-hydrogen exchange regulatory cofactor NHE-RF2 (NHERF-2) also known as tyrosine kina
It employs one cofactor, nicotinamide D-ribonucleotide.
Specifically the cofactor of the (i, j) entry of a matrix, also known a
Cofactor of BRCA1, also known as COBRA1, is a human ge
MOCOS sulfurates the molybdenum cofactor of xanthine dehydrogenase (XDH) and aldehyde
e moiety is then transferred to the lipoamide cofactor of the H protein.
Cofactor of BRCA1 has been shown to interact with Estr
A positive Shannon cofactor of function F with respect to variable x is d
aldehydes, especially the pyridoxal phosphate cofactor of many Vitamin B6-dependent enzymes.
erin (INN) is a naturally occurring essential cofactor of the three aromatic amino acid hydroxylase
The current QS record is a 135-digit cofactor of 2803 − 2402 + 1, itself an Aurifeuillian f
announced that they had factored a 164-digit cofactor of 21826+1.
l. announced the factorisation of a 158-digit cofactor of 2953+1, using a couple of months on about
It acts mainly as a cofactor on coagulation and inflammation, and has no i
light, rhodopsin splits into a protein and a cofactor: opsin and all-trans-retinal (a form of vitam
It employs one cofactor, PQQ.
em (including factor H, factor I and membrane cofactor protein), with the factor H mutations being t
fI cleavage substrates (C3b and C4b) and the cofactor proteins needed for cleavage of C3b (Factor H
It employs one cofactor, pyridoxal phosphate.
uses a covalently bound pyruvate residue as a cofactor rather than the more common pyridoxal 5'-phos
ibes an atom as belonging to a small molecule cofactor rather than to part of a biopolymer chain.
THB is an essential cofactor required by the aromatic amino acid hydroxyla
Aside from its cofactor role for intracellular enzymes, FA also displ
enzymes so far identified in nature use this cofactor, save for the phylogenetically ancient molybd
ed mutations that experimentally switched the cofactor specificity of Candida boidinii xylose reduct
Factor I requires a C3b-binding protein cofactor such as complement factor H, CR1 and Membrane
Molybdenum cofactor sulfurase is an enzyme that in humans is enco
It is restored to the required cofactor tetrahydrobiopterin by dihydrobiopterin reduc
cerol monooxygenase critically depends on the cofactor tetrahydrobiopterin and iron.
It has one cofactor: the flavin FAD.
It employs one cofactor, thiamin diphosphate.
onins are not thought to utilize a GroES-type cofactor to fold their substrates.
The first organic cofactor to be discovered was NAD+, which was identifi
meaning that it uses inorganic phosphate as a cofactor to cleave nucleotide-nucleotide bonds, releas
coagulation pathway, where it functions as a cofactor to Protein C in the inactivation of Factors V
(coupled to ADP) in a step that activates the cofactor toward binding Mo or W.
It employs one cofactor, zinc.