Determination of the Absolute Configuration of Side Chains of Basic Amino Acid Residues Using the Water-Soluble Porphyrin-Based Exciton Chirality Method

2016 ◽  
Vol 120 (39) ◽  
pp. 10280-10287 ◽  
Author(s):  
Shingo Hattori ◽  
Kengo Akagawa ◽  
Kazuaki Kudo ◽  
Kazuyuki Ishii
Keyword(s):  
Amino Acid ◽  
Absolute Configuration ◽  
Basic Amino Acid ◽  
Water Soluble ◽  
Side Chains ◽  
Amino Acid Residues ◽  
The Absolute ◽  
Water Soluble Porphyrin

Determination of the Complete Absolute Configuration of Petriellin A

2006 ◽  
Vol 59 (6) ◽  
pp. 407 ◽  
Author(s):  
Luigi Aurelio ◽  
Robert T. C. Brownlee ◽  
Jason Dang ◽  
Andrew B. Hughes ◽  
Gideon M. Polya
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Natural Product ◽  
Absolute Configuration ◽  
Structural Determination ◽  
Amino Acid Residues ◽  
The Common ◽  
The Absolute ◽  
Derivatives Of

We report the full structural determination of the depsipeptide petriellin A. The absolute configuration of the amino acid residues, N-methyl isoleucine and N-methyl threonine, have been determined by a combination of HPLC and TLC comparison of synthetic Marfey’s derivatives and Marfey’s derivatives of the natural product hydrolysate. The configuration of the chiral centres in these two N-methylated residues was found to be the same as those of the common unmethylated l-amino acids.

scholarly journals Absolute Stereochemistry of the β-Hydroxy Acid Unit in Hantupeptins and Trungapeptins

2016 ◽  
Vol 11 (1) ◽  
pp. 1934578X1601100 ◽  
Author(s):  
Deepak Kumar Gupta ◽  
Gary Chi Ying Ding ◽  
Yong Chua Teo ◽  
Lik Tong Tan
Keyword(s):  
Amino Acid ◽  
Structural Feature ◽  
Absolute Configuration ◽  
Hydroxy Acid ◽  
Hplc Analysis ◽  
The Absolute ◽  
Absolute Stereochemistry ◽  
Common Structural Feature ◽  
Acid Unit

The β-hydroxy/amino acid unit is a common structural feature of many bioactive marine cyanobacterial depsipeptides. In this study, the absolute stereochemistry of the β-hydroxy acid moieties in hantupeptins and trungapeptins were determined through their synthesis and HPLC analysis of the Mosher ester derivatives. Synthesis of two3-hydroxy-2-methyloctanoic acid (Hmoa) stereoisomers, (2 S,3 R)-Hmoa and (2 S,3 S)-Hmoa, were achieved using diastereoselective asymmetric method and the retention times of all four Hmoa isomers were established indirectly by RPLC-MS analysis of their Mosher ester derivative standards. Based on the retention times of the standards, the absolute configuration of the Hmoa unit in hantupeptin C (3) and trungapeptin C (6) was assigned as (2 R,3 S)- and (2 S,3 R)-Hmoa, respectively. The use of the Mosher's reagents, coupled with HPLC analysis, provided a viable alternative to the absolute stereochemical determination of β-hydroxy acid units in depsipeptides.

CD exciton chirality method for determination of the absolute configuration of ?-hydroxy-?-amino acid derivatives

Chirality ◽  
2001 ◽  
Vol 13 (5) ◽  
pp. 266-271 ◽  
Author(s):  
Lee-Chiang Lo ◽  
Jean-Yin Chen ◽  
Chun-Tzu Yang ◽  
Der-Shang Gu
Keyword(s):  
Amino Acid ◽  
Absolute Configuration ◽  
Amino Acid Derivatives ◽  
Hydroxy Amino Acid ◽  
Hydroxy Amino ◽  
The Absolute

scholarly journals cDNA cloning and amino acid sequence of human mitochondrial Δ3Δ2-enoyl-CoA isomerase: comparison of the human enzyme with its rat counterpart, mitochondrial short-chain isomerase

1994 ◽  
Vol 300 (1) ◽  
pp. 1-5 ◽  
Author(s):  
J M Kilponen ◽  
H M Häyrinen ◽  
M Rehn ◽  
J K Hiltunen
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Basic Amino Acid ◽  
Peptide Sequencing ◽  
Amino Acid Residues ◽  
Mature Protein ◽  
Nucleotide Level ◽  
Sequence Identity ◽  
Human Enzyme

We report the isolation of a cDNA encoding a mature human monofunctional delta 3 delta 2-enoyl-CoA isomerase and the determination of its nucleotide sequence. The purified uncleaved protein, as well as several internal tryptic and CNBr fragments, were subjected to N-terminal peptide sequencing. The deduced amino acid sequence of the mature protein consists of 260 amino acids with a predicted M(r) of 28735. The human mitochondrial isomerase exhibits a 74% (78%) sequence identity with the corresponding rat counterpart at amino acid (nucleotide) level(s). Many basic amino acid residues in rat isomerase have been changed to acidic or neutral residues in human enzyme, explaining the differences observed between these proteins.

scholarly journals Primary- and secondary-structural analysis of a unique prokaryotic metallothionein from a Synechococcus sp. cyanobacterium

1988 ◽  
Vol 251 (3) ◽  
pp. 691-699 ◽  
Author(s):  
R W Olafson ◽  
W D McCubbin ◽  
C M Kay
Keyword(s):  
Amino Acid ◽  
Metal Binding ◽  
Helical Structure ◽  
Basic Amino Acid ◽  
Cysteine Residues ◽  
Amino Acid Residues ◽  
C Terminus ◽  
Empirical Relations ◽  
Heavy Metal Binding ◽  
Synechococcus Sp

Biochemical and physiological studies of Synechococcus cyanobacteria have indicated the presence of a low-Mr heavy-metal-binding protein with marked similarity to eukaryotic metallothioneins (MTs). We report here the characterization of a Synechococcus prokaryotic MT isolated by gel-permeation and reverse-phase chromatography. The large number of variants of this molecule found during chromatographic separation could not be attributed to the presence of major isoproteins as assessed by amino acid analysis and amino acid sequencing of isoforms. Two of the latter were shown to have identical primary structures that differed substantially from the well-described eukaryotic MTs. In addition to six long-chain aliphatic residues, two aromatic residues were found adjacent to one another near the centre of the molecule, making this the most hydrophobic MT to be described. Other unusual features included a pair of histidine residues located in repeating Gly-His-Thr-Gly sequences near the C-terminus and a complete lack of association of hydroxylated residues with cysteine residues, as is commonly found in eukaryotes. Similarly, aside from a single lysine residue, no basic amino acid residues were found adjacent to cysteine residues in the sequence. Most importantly, sequence alignment analyses with mammalian, invertebrate and fungal MT sequences showed no statistically significant homology aside from the presence of Cys-Xaa-Cys structures common to all MTs. On the other hand, like other MTs, the prokaryotic molecule appears to be free of alpha-helical structure but has a considerable amount of beta-structure, as predicted by both c.d. measurements and the Chou & Fasman empirical relations. Considered together, these data suggested that some similarity between the metal-thiolate clusters of the prokaryote and eukaryote MTs may exist.

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