「Histidine」の共起表現一覧(1語右で並び替え)
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odopsin gene, in which proline is changed to | histidine, accounts for the largest fraction of rhodop |
also requires that alpha subunits contain a | histidine amino acid residue, (i.e., α1, α2, α3, and α |
Vertebrate c type cytochromes also arrange a | histidine amino acid next to this sequence so that CXX |
Other names in common use include | histidine aminotransferase, and histidine-2-oxoglutara |
Histidine ammonia-lyase is a cytosolic enzyme catalyzi | |
Histidine ammonia-lyase (or histidase, or histidinase) | |
three aminoacylation specificities, valine, | histidine and tyrosine. |
The catalytic | histidine and stabilizing serine residues are colored |
sugar, whereas its two products are protein | histidine and sugar phosphate. |
he positive imidazolium ion of the catalytic | histidine and the negatively charged carboxyl-group of |
he positive imidazolium ion of the catalytic | histidine and the negatively charged carboxyl-group of |
py the first anticodon position of tRNAs for | histidine, aspartic acid, asparagine and tyrosine. |
ADH1B is rs1229984, that changes arginine to | histidine at residue 47. |
glutamic acid; this may reduce the amount of | histidine available for decarboxylation and protein sy |
tore the OH to serine and turn nitrogen from | histidine back into its R3N form (tertiary nitrogen). |
The | histidine bound heme group of succinate dehydrogenase, |
this bond move to attack the hydrogen of the | histidine, breaking the connection. |
It inhibits the | histidine decarboxylase in rats. |
miminoglutamase catalyses the fourth step in | histidine degradation, acting to hydrolyse N-formimido |
rginine/agmatine metabolism, the urea cycle, | histidine degradation, and other pathways. |
sion of a gene encoding proteins involved in | histidine expression in order to survive (Joung et al. |
ds co-ordinating the metal ion can vary with | histidine, glutamate, aspartate, lysine and arginine. |
nine (or ophidine) (beta-alanyl-N tau-methyl | histidine) has been identified in the muscles of sever |
emia is characterized by increased levels of | histidine, histamine and imidazole in blood, urine and |
chosen for the chemical labelling of active | histidine in enzyme analysis. |
However, copper | histidine injections have been shown ineffective in st |
so a form of bovine β-Casomorphin 8 that has | histidine instead of proline in position 8, depending |
Histidase converts | histidine into ammonia and urocanic acid. |
H is a conserved | histidine involved in zinc coordination, |
The transfer RNA (tRNA) for | histidine is unique among eukaryotic tRNAs in requirin |
The imidazole ring of | histidine is aromatic at all pH values. |
Anserine (beta-alanyl-N-methyl | histidine) is found in the skeletal muscle and brain o |
In catalytic triads, the basic nitrogen of | histidine is used to abstract a proton from serine, th |
The imidazole sidechain of | histidine is a common coordinating ligand in metallopr |
Peptide PHI (or peptide | histidine isoleucine) is a peptide which functions as |
carbon moves to attack the hydrogen that the | histidine just acquired. |
otein-L-histidine N-tele-phosphotransferase, | histidine kinase (ambiguous), histidine protein kinase |
In terms of enzymology, a | histidine kinase (EC 2.7.13.3) is an enzyme that catal |
The mechanism for the reactions catalyzed by | histidine kinase have not been completely elucidated, |
Histidine kinases are also found in plants, fungi and | |
t phosphorylate other amino acids, including | histidine kinases that phosphorylate histidine residue |
Histidine kinases are structurally distinct from most | |
inases in animals is structurally related to | histidine kinases, but instead phosphorylate serine re |
nge between armI and armII contains both the | histidine loop and the Q-loop, making contact with the |
alanine, asparagine, aspartic acid, glycine, | histidine, lysine, phenylalanine, proline, serine, and |
This enzyme participates in | histidine metabolism and aminoacyl-trna biosynthesis. |
This enzyme participates in | histidine metabolism and glyoxylate and dicarboxylate |
enzyme participates in 5 metabolic pathways: | histidine metabolism, tyrosine metabolism, phenylalani |
olic pathways: glycolysis / gluconeogenesis, | histidine metabolism, tyrosine metabolism, phenylalani |
no groups, alanine and aspartate metabolism, | histidine metabolism, and beta-alanine metabolism. |
s, glycine, serine and threonine metabolism, | histidine metabolism, tyrosine metabolism, phenylalani |
isoleucine degradation, lysine degradation, | histidine metabolism, tryptophan metabolism, beta-alan |
This enzyme participates in | histidine metabolism. |
It is a secondary disorder of | histidine metabolism. |
anserine, preferring dipeptides that have a | histidine monomer in the c-terminus position. |
both of which are characterized by conserved | histidine motifs. |
The | histidine phosphorylation site is located at His-260. |
h normal to only slightly elevated levels of | histidine present in the liver during urocanic aciduri |
In a | histidine proton shuttle, histidine is used to quickly |
In carbonic anhydrases, a | histidine proton shuttle is utilized to rapidly shuttl |
consists of 118 amino acid residues" or "The | histidine residue is considered to be basic due to its |
phosphate group from ATP is first added to a | histidine residue within the kinase, and later transfe |
rate is released with an amine terminus, the | histidine residue in the protease is restored to its d |
fth haem iron ligand is always provided by a | histidine residue. |
mino acid with a basic side chain, usually a | histidine residue. |
nd α6 subunits with an arginine instead of a | histidine residue. |
erring a phosphate group to the sidechain of | histidine residues in proteins (protein-histidine kina |
Just two | histidine residues and one aspartic acid residue are e |
The zinc ion (green) is coordinated by two | histidine residues and two cysteine residues. |
e four copper atoms are coordinated by seven | histidine residues and bridged by a sulfur atom. |
Several highly conserved | histidine residues were found in the zinc binding moti |
up of Rob Liskamp have shown that scaffolded | histidine residues can be used as mimics of certain me |
cant improvement since the use of scaffolded | histidine residues is one step closer to the mimicry o |
Besides the precisely placed glutamate and | histidine residues to form the enediol, a ten- or elev |
ore, it is highly significant that these two | histidine residues, His214 and His270, and one asparti |
of the enzyme is coordinated by at least two | histidine residues, an aspartate residue, a glutamine |
2+ or Cu+, coordinated tetrahedrally by four | histidine residues. |
omain named after its three highly conserved | histidine residues. |
of copper centres, each coordinated by three | histidine residues. |
c (light blue) is shown coordinated to three | histidine residues. |
s appears to be conferred by the presence of | histidine side chains in the extracellular domain. |
e HIS3 gene, encoding a protein required for | histidine synthesis, the LEU2 gene, encoding a protein |
There is also a conserved | histidine that is likely to be an active site residue. |
The amino acid | histidine, the signaling molecule histamine, and the p |
In enzymology, a | histidine transaminase (EC 2.6.1.38) |
stidyl-transfer ribonucleate synthetase, and | histidine translase. |
n aspartic acid residues (in contrast to one | histidine, two lysine and three arginine residues) is |
s enzyme are phosphoenolpyruvate and protein | histidine, whereas its two products are pyruvate and p |
known that the imidazole ring is supplied by | histidine, which is then methylated to produce histidi |
dination bond to an evolutionarily-conserved | histidine, while nitric oxide synthase and cytochrome |
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