「Leucine」の共起表現(1語右で並び替え) - Weblio英語共起表現検索


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「Leucine」の共起表現一覧(1語右で並び替え)

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r very short peptide sequence that is rich in leucine amino acid.
include norleucine transaminase, norleucine ( leucine) aminotransferase, and leucine L-norleucine:
responsible for the third step in processing leucine, an essential amino acid.
lly, the enzyme is responsible for processing leucine, an amino acid that is part of many proteins.
l group performing the 4th step in processing leucine, an essential amino acid.
Only leucine and lysine are not glucogenic.
This enzyme participates in valine, leucine and isoleucine degradation and valine, leucin
leucine and isoleucine), accurate manual sequencing c
This enzyme participates in valine, leucine and isoleucine degradation.
participates in 3 metabolic pathways: valine, leucine and isoleucine degradation, valine, leucine a
Leucine and isoleucine belong to the proteinogenic am
This enzyme participates in valine, leucine and isoleucine biosynthesis and c5-branched d
This enzyme participates in valine, leucine and isoleucine biosynthesis and pantothenate
This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trn
olic pathways: fatty acid metabolism, valine, leucine and isoleucine degradation, and butanoate met
ition in the pentapeptide repeat is usually a leucine and has been designated as position i.
participates in 3 metabolic pathways: valine, leucine and isoleucine degradation, beta-alanine meta
ys: alanine and aspartate metabolism, valine, leucine and isoleucine degradation, beta-alanine meta
by crystallizing the two together, along with leucine and the respective 2 sodium ions.
, is a metabolite of the essential amino acid leucine and is synthesized in the human body.
tructure forms when the cell has an excess of leucine and ribosome movement over the leader transcr
phosphatidic acid, amino acids (particularly leucine), and oxidative stress.
ional modification including epimerization of leucine and tryptophan, tryptophan bromination, amida
sis and degradation of ketone bodies, valine, leucine and isoleucine degradation, lysine degradatio
cycle and metabolism of amino groups, valine, leucine and isoleucine degradation, lysine degradatio
f the branched-chain amino acids, isoleucine, leucine, and valine, is catalyzed by the branched-cha
functional group, though sometimes Valine and Leucine are used when conservation of the size of mut
t slower rates, particularly those containing leucine at the P1 position.
that contain phenylalanine codons instead of leucine codons, and are upstream of genes involved in
Known also as the heptad repeat, one leucine comes in direct contact with another leucine
In enzymology, a leucine dehydrogenase (EC 1.4.1.9)
L-Alanine is second only to leucine in rate of occurrence, accounting for 7.8% of
erentially transports branched-chain (valine, leucine, isoleucine) and aromatic (tryptophan, tyrosi
entially transports neutral branched (valine, leucine, isoleucine) and aromatic (tryptophan, tyrosi
are primarily the four isomeric amino acids: leucine, isoleucine, tert-leucine and norleucine.
e synthesis of the branched chain amino acids leucine, isoleucine, and valine(2).
tially the same as a previously characterized leucine leader in the same species.
L405 ( leucine located at residue 405) located in the substr
shown to preferentially cleave proteins after leucine, methionine, and phenylalanine residues.
steine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan and valine
be unable to fully break down isoleucine and leucine molecules .
A change in codon 102 from proline to leucine on chromosome 20, has been found in the prion
The Leucine operon leader is an RNA element found upstrea
ing frame (ORF) that contains many codons for leucine or phenylalanine.
he amino acid sequence is N-formylmethionine, leucine, phenylalanine.
this enzyme, the body is unable to break down leucine properly.
Furthermore, the hydrophobic leucine region is absolutely required for DNA binding
The leucine residues that represent the 'teeth' of the zi
the UL-6 amino acid sequence demonstrated the leucine residues in a predicted leucine zipper motif
It is characterized by the presence of two leucine residues in its N-terminal intracellular doma
e receptor, within the pore lumen, valine and leucine residues (Val 255 and Leu 251) define a hydro
PELP-1 (proline, glutamic acid and leucine rich protein 1) PELP1
as nucleotide-binding oligomerization domain, leucine rich repeat and CARD domain containing 3 (NOD
or nucleotide-binding oligomerization domain, leucine rich repeat containing X1, is an intracellula
he LEU2 gene, encoding a protein required for leucine synthesis and the URA3 gene, encoding a prote
rleucine (abbreviated as Nle) is an isomer of leucine, the α-amino acid 2-amino-hexanoic acid.
se to form HMG-CoA. (During the metabolism of leucine, this last reaction is reversed.)
en in D-BP deficiency patients is caused by a leucine to proline substitution.
CC performs a single step in the breakdown of leucine to eventually yield acetyl CoA and acetoaceta
In enzymology, a leucine transaminase (EC 2.6.1.6)
acid synthetase, leucine-tRNA synthetase, and leucine translase.
A single leucine zipper consists of multiple leucine residues
Maternal embryonic leucine zipper kinase is an enzyme that in humans is
transcription factor that is a member of the leucine zipper family of DNA-binding proteins.
The leucine zipper is a super-secondary structure that fu
loop-helix, zinc finger, helix-turn-helix and leucine zipper motifs have been used in construction
ongs to the cap'n'collar type of basic region leucine zipper factor family (CNC-bZip).
These genes encode leucine zipper proteins that can dimerize with protei
Basic leucine zipper and W2 domain-containing protein 1 is
e through hydrogen bonding, and a hydrophobic leucine zipper region that is responsible for dimeriz
a basic region involved in DNA binding and a leucine zipper motif involved in dimerization.
f a zinc finger and one motif suggestive of a leucine zipper in which 1 cysteine is found instead o
Leucine Zipper (blue) bound to DNA.
ZIP (Proline and Acidic amino acid-Rich basic leucine ZIPper) transcription factor family.
verhead view", or helical wheel diagram, of a leucine zipper, where d represent amino acid leucine
n, while the dimeric structure is formed by a leucine zipper.
                                                                                                   


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