「phenylalanine」の共起表現(2語左で並び替え)

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共起表現

「phenylalanine」の共起表現一覧(2語左で並び替え)

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ynthesized from tyrosine or a hydroxylated	phenylalanine.
As a result,	phenylalanine from the diet builds up in the bloodstream
acids as are the aromatic amino acid pair,	phenylalanine and tyrosine.
esis of the aromatic amino acids tyrosine,	phenylalanine, and tryptophan.
are derived from aromatic amino acids like	phenylalanine, tyrosine, tryptophan, and the thyroid hor
lps convert several amino acids, including	phenylalanine, to other essential molecules in the body.
similar to the two amino acids alanine and	phenylalanine.
an inability to break down the amino acid	phenylalanine due to an hereditary deficiency of the nec
strongly elevated levels of the amino acid	phenylalanine in the blood.
synthesized by plants from the amino acid	phenylalanine.
e biosynthesis of the aromatic amino acids	phenylalanine and tyrosine.
rotein composed entirely of the amino acid	phenylalanine.
RNA codons, which coded for the amino acid	phenylalanine.
mes, used in the degradation of amino acid	phenylalanine and in the biosynthesis of the neurotransm
The aromatic amino acids	phenylalanine and tyrosine
"Xxx" is either an aromatic (	phenylalanine, tyrosine) or a branched aliphatic (valine
Analogously to	phenylalanine hydroxylase and tyrosine hydroxylase, this
idual components, including aspartic acid,	phenylalanine, methanol, and further breakdown products
amicidin A contains Tryptophan, B contains	Phenylalanine and C contains Tyrosine.
and II cleave hemoglobin between residues	Phenylalanine 33 and Leucine 34 of α-globin subunit.
ic code is read in triplets, the codon for	phenylalanine is UUU.
EA5 patients have a cysteine to	phenylalanine mutation at position 104.
ase (deaminating and decarboxylating), and	phenylalanine (deaminating, decarboxylating)oxidase.
ants, ferulic acid (right) is derived from	phenylalanine, which is converted to 4-hydroxycinnamic a
s (two ending in glycine and two ending in	phenylalanine), with the chains cross-linked by disulfid
In enzymology, a	phenylalanine 2-monooxygenase (EC 1.13.12.9) is an enzym
In enzymology, a	phenylalanine adenylyltransferase (EC 2.7.7.54) is an en
In enzymology, a	phenylalanine N-acetyltransferase (EC 2.3.1.53)
d by a special diet with highly restricted	phenylalanine content.
aspartic acid, glycine, histidine, lysine,	phenylalanine, proline, serine, and threonine belong to
on-enzymatic free-radical hydroxylation of	phenylalanine under conditions of oxidative stress.
Other names in common use include tyrase,	phenylalanine deaminase, tyrosine ammonia-lyase, L-tyros
It is involved in	phenylalanine, tryptophan, and alkaloid production, and
) that contains many codons for leucine or	phenylalanine.
With a special diet low in	phenylalanine, PKU newborns can grow and develop into no
me participates in tyrosine metabolism and	phenylalanine metabolism.
ve proteins after leucine, methionine, and	phenylalanine residues.
d sequence is N-formylmethionine, leucine,	phenylalanine.
This enzyme participates in	phenylalanine, tyrosine and tryptophan biosynthesis and
This enzyme participates in	phenylalanine, tyrosine and tryptophan biosynthesis and
This enzyme participates in	phenylalanine, tyrosine and tryptophan biosynthesis and
This enzyme participates in	phenylalanine metabolism.
This enzyme participates in	phenylalanine, tyrosine and tryptophan biosynthesis.
This enzyme participates in	phenylalanine metabolism and phenylpropanoid biosynthesi
This enzyme participates in	phenylalanine and tryptophan metabolism.
Protegrin-4 substitutes a	phenylalanine for a valine at position 14 and sequences
metabolism of aromatic amino acids such as	phenylalanine and tyrosine.
nd preferably aromatic amino acids such as	phenylalanine, tryptophan, and tyrosine.
f cinnamic acid, which is synthesized from	phenylalanine in the first step of phenylpropanoid biosy
enzyme found to use tetrahydrobiopterin is	phenylalanine hydroxylase (PAH).
ional homologs were uncovered that contain	phenylalanine codons instead of leucine codons, and are
a centrally-acting inhibitor of the enzyme	phenylalanine hydroxylase (PH).
In analogy to the enzymes	phenylalanine hydroxylase, tyrosine hydroxylase, tryptop
hesis is performed by action of the enzyme	phenylalanine ammonia-lyase (PAL) on phenylalanine.
atic amino acids tyrosine, tryptophan, and	phenylalanine.
P1 position) is a tyrosine, tryptophan, or	phenylalanine.
ethionine metabolism, tyrosine metabolism,	phenylalanine metabolism, phenylalanine, tyrosine and tr
histidine metabolism, tyrosine metabolism,	phenylalanine metabolism, phenylalanine, tyrosine and tr
ver, the body can synthesise tyrosine from	phenylalanine, an essential amino acid.
5 metabolic pathways: tyrosine metabolism,	phenylalanine metabolism, nitrogen metabolism, phenylpro
histidine metabolism, tyrosine metabolism,	phenylalanine metabolism, and metabolism of xenobiotics
histidine metabolism, tyrosine metabolism,	phenylalanine metabolism, tryptophan metabolism, beta-al
This enzyme participates in tyrosine and	phenylalanine catabolism.
ine, isoleucine, methionine, tyrosine, and	phenylalanine.
form chorismate which can then be used in	phenylalanine, tyrosine or tryptophan biosynthesis.

共起表現

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「phenylalanine」の共起表現一覧(2語左で並び替え)