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Sentences for "aspartate "
0 grammes Potassium aspartate 3.
In accordance with metal-ATP complex coordination on other enzymes that hydrolyze ATP, like F 1 -ATPase [ 22 28 ] , the ?
- and ß-phosphate of ATP most likely bind to VO 2+while the third carboxyl group is contributed by a side-chain of aspartate or glutamate of sCD39.
Thus one amino group from lysine, one carboxyl group from aspartate or glutamate, and two oxygens from the phosphates of ADPNP serve as the equatorial ligands of sCD39 bound VO 2+in the presence of ADPNP.
Dephosphorylation of these threonines is a prerequisite of filament assembly, as confirmed by the phenotypes of a 3xAsp mutant, in which the three threonines are replaced by three aspartate residues (mimicking the phosphorylated state) [ 11 ] .
We also verified that the unique behavior of the Rab24 mutant was not related specifically to the substitution at the aspartate position in the N(T)KxD motif.
1 sequence, include in sequential order: 1) A DxxTTxxDxxWR motif immediately preceding M1, 2) a highly conserved tryptophan in M1, 3) an insertion in the M1-P loop that contains a CVxx (V or I) motif, 4) the absence of an aromatic residue at the first 'aromatic cuff position [ 2 ] in the P segment helix, 5) a glutamine near the end of the P helix, 6) the absence of an aspartate at the end of the P segment signature sequence (TVGYGD) and a RxxTxxCP motif in the P-M2 loop that is two residues longer than in most other K +channels, 7) a glutamine in the first part of S6, and 8) a hydrophilic residue (Asn, Asp, or Glu) near the mid region of S6 that when negatively charged is involved in blockade of some Kir's by Mg 2+ [ 9 ] .
The second residue is retained as either a glutamate in PCP-2 and RPTPµ, or an aspartate in RPTP?
.
This AAA domain is connected by a large linker domain to a D/E-rich domain that has a conserved amino acid composition rich in aspartate and glutamate residues, but only moderately conserved sequence.
It is characterized by having a highly acidic amino acid composition, with 35-40% of the residues being either aspartate or glutamate (Fig.
One possibility is that the MIDAS site serves to attach protein ligands through a mechanism involving participation of a glutamate or aspartate residue on the ligand in the coordination of a Mg 2+ion at the MIDAS site of midasin, in a manner similar to that by which the MIDAS site in integrin I-domains appears to mediate attachment of collagen through the glutamate in the GFOGER binding motif [ 36 ] .
The D/E-rich domain is reduced in size by ~50%, while retaining its acidic character with a high percentage of aspartate and glutamate residues.
To identify amino acids critical for FtsZ function, we constructed 16 mutations, mostly changing conserved aspartate and glutamate residues to alanine.
16 more results not shown.
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