Partial Amino Acid Sequence of Crayfish (Astacus Leptodactylus) Hemocyanin

Schneider, H.‐J.; Voll, Wolfgang; Lehmann, Lars; Grisshammer, Reinhard; Goettgens, A.; Linzen, Bernt

doi:10.1007/978-3-642-71481-8_31

Cited by 9 publications

(4 citation statements)

References 8 publications

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“…In contrast to the lobster and the spiny lobster where all subunits are glycosylated, there is only one subunit glycosylated in A. leptodactylus hemocyanin. Subunit b of Astacus hemocyanin, which shows a high degree of sequence similarity to the subunit a of the Panulirus hemocyanin (Gaykema et al, 1984;Bak et al, 1986;Neuteboom et al, 1986Neuteboom et al, , 1992Schneider et al, 1986;Soeter et al, 1986;Jekel et al, 1988;Volbeda and Hoi, 1988) has at the corresponding glycosylation site (Asn-X-Ser/Thr) in domain 1 an exchange of amino acids Asn-Val-Ser from Panulirus to Asn-MetAsp (Schneider ef al., 1986) and is therefore not glycosylated, as demonstrated here. The glycosylation site(s) in A leptodactylus hemocyanin are not yet known, since with the exception of a part of subunit b, no other subunits are sequenced till now.…”

Section: Resultsmentioning

confidence: 97%

Characterization of N-Linked Carbohydrate Chains of the Crayfish,Astacus leptodactylusHemocyanin

Tseneklidou‐Stoeter¹,

Gerwig²,

Kamerling³

et al. 1995

Biological Chemistry Hoppe-Seyler

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The primary structure of the carbohydrate chains of hemocyanin from the crayfish Astacus leptodactylus were investigated. The carbohydrate content is 0.2% (w/w) as referred to total hemocyanin content, resp. 1.8% as referred only to the one subunit which is glycosylated. Mannose and N-acetylglucosamine are present in a molar ratio of 6:2. The carbohydrate chains are N-glycosidically linked as revealed by dot blot analysis using various lectins and enzymatic deglycosylation. Furthermore, they are part of only one hemocyanin subunit of A. leptodactylus. After enzymatic deglycosylation with PNGase F, the oligosaccharide pool was separated by FPLC on Mono Q and subsequent HPLC on Lichrosorb-NH2, the subfractions were characterized by 1H NMR spectroscopy. A total of six oligosaccharides, ranging from Man4GlcNAc2 to Man9GlcNAc2 is present, Man6GlcNAc2 representing the most abundant one with 57% of all oligosaccharides.

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Section: Resultsmentioning

confidence: 97%

Characterization of N-Linked Carbohydrate Chains of the Crayfish,Astacus leptodactylusHemocyanin

Tseneklidou‐Stoeter¹,

Gerwig²,

Kamerling³

et al. 1995

Biological Chemistry Hoppe-Seyler

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“…The sequence coverage was 2%, residues matching from 235 to 248, and 234 to 248, respectively. Another peptide at 1320.7 m/z also showed some homology with a hemocyanin B chain from narrow-fingered crayfish (Astacus leptodactylus), with a 75% sequence matching a similar length fragment of this protein (Schneider, Voll, Lehmann, Grisshammer, Goettgens, & Linzen, 1986). The peptides at 1512.7 and 1698.8 m/z were sequenced de novo.…”

Section: Mass Spectrometrymentioning

confidence: 99%

Presence of hemocyanin with diphenoloxidase activity in deepwater pink shrimp (Parapenaeus longirostris) post mortem

Martínez-Álvarez¹,

Gómez‐Guillén²,

Montero³

2008

Food Chemistry

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Polyphenoloxidase and hemocyanin are two proteins which although very similar perform different physiological functions in crustaceans. This paper reports the presence of 15 hemocyanin with diphenoloxidase activity in deepwater pink shrimp (Parapenaeus longirostris) post mortem. Polyacrylamide gels and specific inhibitors and substrates of 17 mono-and diphenoloxidases were used for purposes of recognition, and MALDI-TOF mass 18 spectrometry for identification. Presumptive polyphenoloxidase was found in an inactive 19 form in cephalothorax following capture, subsequently becoming active during storage. Also 20 in the course of storage, hemocyanin acquired the ability to oxidize diphenols. Ascorbic acid, 21 sodium metabisulphite and tropolone inhibited the prooxidant activity of both presumptive polyphenoloxidase and hemocyanin in the gels. 4-hexylresorcinol did not avoid the appearance of activity bands in the gel corresponding with hemocyanin, maybe because 4hexylresorcinol is described as slow-binding inhibitor. The acquired prooxidant activity of hemocyanin following capture is especially important because of the rapid development of melanosis in deepwater pink shrimp during storage.

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“…These molecules do not transport oxygen, but function as amino acid stores rich in aromatic residues or methionine. Accordingly, the class of insect storage proteins provides us with an elegant method for investigating whether a residue is conserved for structural Gaykema et al (1984); SS PINT A = position of helices (A) and &strands (B) in the Panulirus structure; NR PINT A = sequence numbering for Panulirus hemocyanin; PINT C = Panulirus interruptus C-chain (Neuteboom et al, 1992); ALEP B = Astacus leptodactylus B-chain (Schneider et al, 1986); PVUL B = Pulinurus vulgaris B-chain (Neuteboom et al, 1989); PlNT A = Panulirus interruptus A-chain (Bak …”

Section: B Hazes Et Almentioning

confidence: 99%

Crystal structure of deoxygenated limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation

et al. 1993

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The crystal structure of Limulus polyphemus subunit type I1 hemocyanin in the deoxygenated state has been determined to a resolution of 2.18 A . Phase information for this first structure of a cheliceratan hemocyanin was obtained by molecular replacement using the crustacean hemocyanin structure of Panulirus interruptus. The most striking observation in the Limulus structure is the unexpectedly large distance of 4.6 A between both copper ions in the oxygen-binding site. Each copper has approximate trigonal planar coordination by three histidine NE atoms. No bridging ligand between the copper ions could be detected. Other important new discoveries are (1) the presence of a cis-peptide bond between Glu 309 and Ser 310, with the carbonyl oxygen of the peptide plane hydrogen bonded to the N6 atom of the copper B ligand His 324; (2) localization of a chloride-binding site in the interface between the first and second domain; (3) localization of a putative calcium-binding site in the third domain. Furthermore, comparison of Limulus versus Panulirus hemocyanin revealed considerable tertiary and quaternary rigid body movements, although the overall folds are similar. Within the subunit, the first domain is rotated by about 7.5" with respect to the other two domains, whereas within the hexamer the major movement is a 3.1 O rotation of the trimers with respect to each other. The rigid body rotation of the first domain suggests a structural mechanism for the allosteric regulation by chloride ions and probably causes the cooperative transition of the hexamer between low and high oxygen affinity states. In this postulated mechanism, the fully conserved Phe 49 is the key residue that couples conformational changes of the dinuclear copper site into movements of the first domain.

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Partial Amino Acid Sequence of Crayfish (Astacus Leptodactylus) Hemocyanin

Cited by 9 publications

References 8 publications

Characterization of N-Linked Carbohydrate Chains of the Crayfish,Astacus leptodactylusHemocyanin

Characterization of N-Linked Carbohydrate Chains of the Crayfish,Astacus leptodactylusHemocyanin

Presence of hemocyanin with diphenoloxidase activity in deepwater pink shrimp (Parapenaeus longirostris) post mortem

Crystal structure of deoxygenated limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation

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