The Structures and Absolute Configurations of Anhydrodeoxyheptitols

Camerman, Arthur; Koch, H.; Rosenthal, Alex; Trotter, J.

doi:10.1139/v64-388

Cited by 10 publications

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“…As in the human albumin, the first two or three residues of the structure are disordered. This inferred mobility should provide the flexibility necessary for the chelation of Cu and Ni, since both the His3 and the N-terminal nitrogen are involved in metal coordination [54].…”

Section: Tertiary Structurementioning

confidence: 99%

X‐ray and primary structure of horse serum albumin (Equus caballus) at 0.27‐nm resolution

Holowachuk

Norton

et al. 1993

European Journal of Biochemistry

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The amino-acid sequence and three-dimensional structure of equine serum albumin have been determined. The amino-acid sequence was deduced from cDNA isolated from equine liver. Comparisons of the primary structure of equine serum albumin with human serum albumin and bovine serum albumin reveal 76.1 % and 73.9% sequence identity, respectively. The three-dimensional structure was determined crystallographically by the molecular-replacement method using molecular coordinates from the previously determined structure of human serum albumin, to a resolution of 0.27 nm. In accordance with the primary structure, the three-dimensional structures are highly conserved. There is a root-mean-square difference between a-carbons of the two structures of 0.201 nm. The association constants (Ka) for the binding of 2,3,5-triiodobenzoic acid were determined by ultrafiltration methods for equine and human serum albumins to be approximately 1WM-l and 105M-', respectively. Crystallographic studies of equine serum albumin reveal two binding sites for 2,3,5-triiodobenzoic acid identical with those previously reported for human serum albumin which are located within subdomains IIA and IIIA. Details and comparisons of the binding chemistry are discussed.As the most abundant protein of the circulatory system albumin functions as a multipurpose transport molecule and is a principal contributor to colloid osmotic blood pressure.

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Section: Tertiary Structurementioning

confidence: 99%

X‐ray and primary structure of horse serum albumin (Equus caballus) at 0.27‐nm resolution

Holowachuk

Norton

et al. 1993

European Journal of Biochemistry

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“…The ligands involved in Zn(I1)binding have been identified as His (69), Glu (72), and His (196) (Lipscomb et al, 1968;Bradshaw et al,, 1969). As part of our investigation of molecular design of the functional sites of biological macromolecules (Lau et al, 1974;Lau & Sarkar, 1975;Kruck et al, 1976;Camerman et al, 1976;Sarkar, 1977;Iyer et al,, 1978;Sarkar et al, 1978;Arena et al, 1979; Lakusta el QL, 1980;Laussac & Sarkar, 1980~. b), the Zn(I1)-binding site of carboxypeptidase was studied.…”

Section: Carboxypeptidasementioning

confidence: 99%

“…8. Earlier design in this laboratory included peptide molecules mimicking the native metalbinding site located on a short sequence of the polypeptide chain (Lau et al, 1974;Lau & Sarkar, 1975;Kruck et al, 1976;Camerman et al, 1976;Sarkar et al, 1976Sarkar et al, , 1978Iyer et al, 1978;Arena et aZ., 1979). The present results show the feasibility of designing peptide molecules mimicking the metal-binding site of a metalloenzyme where the ligands originate from various parts of the polypeptide chain.…”

Section: Zinc(ii)-cyclo-octapeptide Complexmentioning

confidence: 99%

Design, Synthesis and 13 C‐ and 1 H‐N.M.R. Investigation of a Cyclic Octapeptide to Mimic the Zinc‐binding Site of Carboxypeptidase A

Iyer

Laussac

Lau

et al. 1981

International Journal of Peptide and Protein Research

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Considering the three‐dimensional structure and the native Zn(II)‐binding ligands of carboxypeptidase A followed by extensive model building, a cyclic octapeptide, cyclo‐(Gly‐L‐Glu‐Gly‐Gly‐L‐His‐Gly‐L‐His‐Gly) was designed to mimic the Zn(II)‐binding site of carboxypeptidase A. The cyclic octapeptide was prepared by high dilution technique from the corresponding linear octapeptide, N‐Boc‐Gly‐γ‐OBut‐L‐Glu‐Gly‐Gly‐L‐His‐Gly‐L‐His‐Gly‐OBzlNO2 via the azide method. The linear octapeptide was obtained by coupling of the two tetrapeptide fragments: N‐Boc‐Gly‐γ‐OBut‐L‐Glu‐Gly‐Gly‐ONp and L‐His‐Gly‐L‐His‐Gly‐OBzlNO2. The cyclic peptide was purified to homogeneity by the method of countercurrent distribution. The product obtained was both ninhydrin negative and Pauli's reagent positive. Further confirmation of this material was obtained by the proper amino acid ratio of its acid hydrolysate and by the proton magnetic resonance spectrum in which the various kinds of protons of this peptide were accounted for. A detailed 13C‐ and 1H‐n.m.r. investigation was undertaken to determine the Zn(II)‐binding ligands of the cyclo‐octapeptide. The assignments for all the resonances were attempted by pH titration, by employing homonuclear decoupling experiments and by synthesis of cyclo‐octapeptide containing specifically deuterated amino acids cyclo‐(Gly‐L‐Glu‐Gly‐d2‐Gly‐d2‐L‐His‐Gly‐L‐His‐Gly). Titration results of Zn(II) bound form of the cyclic peptide showed the presence of a 1:1 complex. Upon Zn(II)‐binding, the proton resonances were shifted downfield, the largest change being that of the histidine residues and more particularly C(2)‐H protons. The chemical shifts induced on glutamic acid residue were also observed for Glu CH2γ. In the case of 13C resonances, the maximum change in chemical shift was observed in the histidine residues and especially in the imidazole ring upon complexation. Two methylenes of the glutamic acid residue showed a large change in chemical shift upon ligating to the metal ion. The most significant observation was the deshielding effect of the Glu COO‐ group. The results demonstrate that Zn(II) binds both the imidazoles of the two histidine residues and the carboxyl side chain of the glutamic acid residue of the designed cyclic octapeptide.

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“…The latter con~pound had been produced by application of the 0x0 reaction to 3,4,6-tri-0-acetyl-D-glucal (4). The absolute configuration of the 1-0-(p-bromobenzenesulfonyl) derivative (V) had been previously proved by X-ray analysis (4), and (V) has been converted by standard procedures into (VI).…”

mentioning

confidence: 99%

THE REACTION OF UNSATURATED CARBOHYDRATES WITH CARBON MONOXIDE AND HYDROGEN: IV. STRUCTURE AND STEREOCHEMISTRY OF ANHYDRODEOXYHEPTITOLS FROM 3,4,6-TRI-O-ACETYL-D-GALACTAL

Rosenthal¹,

Abson²

1965

Can. J. Chem.

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3,4,6-Tri-0-acetyl-D-galactal reacted with carbon monoxide and hydrogen in the presence of dicobalt octacarbonyl t o yield 2,6-anhydro-3-deoxy-D-galado-heptitol (I) and 2,6-anhydro-3-deoxy-D-lalo-heptitol (11). The stereochemistry of (I) and (11) has been established by correlation with 2,6-anhydro-3-deoxy-D-gluco-heptitol (VI) of lcnown configuration. Evidence that both (I) and (11) are formed by the addition of a hydroxmethyl group t o C-1 of the glycal is also furnished by the proton 1l.m.r. spectra of the normal and deuterated anhydrodeoxyheptitols.Part I of this series (1) described the action of carbon monoxide and hydrogen on 3,4,6-tri-0-acetyl-~-galactal, and presented evidence for the formation of a n anhydrodeoxyheptitol of unknown stereochemistry. I t has since been found t h a t 3,4,6-tri-0-acetyl-D-galactal reacts under 0x0 conditions in a manner entirely analogous t o other glycals investigated (2,3) to yield a s the major products a pair of isomeric anhydrodeoxyheptitols (I) and (11), formed by the addition of a hydroxymethyl group to C-1 of the unsaturated carbohydrate. The stereochemistry of (I) and (11) has been elucidated by a n analysis of their proton n.m.r. spectra and by correlation with 2,6-anhydro-3-deoxy-D-gbco-heptitol (VI), whose structure has been proved by crystallographic X-ray analysis (4).3,4,6-Tri-0-acetyl-D-galactal (5) was reacted in a high-pressure apparatus with carbon monoxide and hydrogen in the presence of dicobalt octacarbonyl, under conditions similar to those described previously (1). The reaction product was separated from the catalyst by chromatography on a Florisil column, and deacetylated with methanolic sodium methoxide. The two major reaction products (I) and (11), after separation by preparative paper chromatography, were obtained in approximately equal amounts. DISCUSSION Both (I) and (11) consumed 1 molar equivalent of periodate (0.95 and 0.98 respectively) as measured by the spectrophotometric method of Dixon and Lipkin (6). Fraction (11) reacted with acetone in the presence of sulfuric acid to form a monoisopropylidene derivative (VII), which on treatment with p-toluenesulfonyl chloride in pyridine gave a compound (VIII) containing two tosyloxy groups. The latter compound on heating with sodiunl iodide in acetone solution liberated 2 equivalents of sodium p-toluenesulfonate. Thus i t is highly likely t h a t (11) contains two primary hydroxyl groups and two adjacent cis secondary hydroxyl groups. Compound (I) was characterized as the tetra-0-(p-nitrobenzoyl) derivative.Evidence that both (I) and (11) have unbranched carbon skeletons was furnished by their proton nuclear magnetic resonance (n.m.r.) spectra, measured in DzO solution (Fig. l a and c). These both show a group of signals a t lower field (3.3-4.3 p.p.m.) with total area corresponding t o 8 hydrogens, and a further group a t higher field (1.3-2.3 p.p.m.), area = 2 hydrogens. The higher field signals can clearly be assigned t o hydrogens attached

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The Structures and Absolute Configurations of Anhydrodeoxyheptitols

Abstract: not available

Cited by 10 publications

References 0 publications

X‐ray and primary structure of horse serum albumin (Equus caballus) at 0.27‐nm resolution

X‐ray and primary structure of horse serum albumin (Equus caballus) at 0.27‐nm resolution

Design, Synthesis and 13 C‐ and 1 H‐N.M.R. Investigation of a Cyclic Octapeptide to Mimic the Zinc‐binding Site of Carboxypeptidase A

THE REACTION OF UNSATURATED CARBOHYDRATES WITH CARBON MONOXIDE AND HYDROGEN: IV. STRUCTURE AND STEREOCHEMISTRY OF ANHYDRODEOXYHEPTITOLS FROM 3,4,6-TRI-O-ACETYL-D-GALACTAL

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