Physicochemical Characteristics and Conformational Features of Alginate Lyase Isozymes from<i>Turbo cornutus</i>

Muramatsu, Tsuyoshi; Hashimoto, Hiroyuki; Takahashi, Tsuyoshi

doi:10.1080/00021369.1984.10866096

Cited by 5 publications

(11 citation statements)

References 6 publications

(6 reference statements)

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“…12 For longer than hexasaccharide, similar catalytic rate constants are observed. These results indicate that the subsite size is appropriate for a hexasaccharide.…”

Section: Active Sitesupporting

confidence: 73%

“…Furthermore, the circular dichroic spectrum studies of 30 Mr class alginate lyases suggested that b-sheets are a major ordered conformation in their tertiary structures. [11][12][13][14] These observations suggested that the tertiary structures of 30 Mr class alginate lyases and 40 Mr class lyases were completely different even though catalytic mechanisms should be involved in enzymes belonging to two classes.…”

Section: Introductionmentioning

confidence: 94%

“…The size of the putative substrate binding site and location of catalytic residues are in good agreement with previous data. 12 As described above, mutational analyses as well as the crystal structure of 1,3-1,4-b-glucanase complex with a suicide inhibitor (PDB code 1byh) defined the catalytic residue as Glu105, which locates in the center of the cleft. Furthermore, comparison of the ALY-1 structure with that of AI-III suggested that Tyr195, His119, Gln117, and Arg72 may be involved in catalytic activity in ALY-1.…”

Section: Active Sitementioning

confidence: 99%

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Crystal Structure of the Alginate (Poly α-l-guluronate) Lyase from Corynebacterium sp. at 1.2Å Resolution

Osawa

Matsubara

Muramatsu

et al. 2005

Journal of Molecular Biology

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“…12 For longer than hexasaccharide, similar catalytic rate constants are observed. These results indicate that the subsite size is appropriate for a hexasaccharide.…”

Section: Active Sitesupporting

confidence: 73%

Section: Introductionmentioning

confidence: 94%

Section: Active Sitementioning

confidence: 99%

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Crystal Structure of the Alginate (Poly α-l-guluronate) Lyase from Corynebacterium sp. at 1.2Å Resolution

Osawa

Matsubara

Muramatsu

et al. 2005

Journal of Molecular Biology

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“…On the other hand, their protein conformations and stabilities toward denaturants, heat, and chemical modifications are distinguishable from each other. The conformation of SP1 is rather looser and more labile (Muramatsu and Egawa, 1982;Muramatsu et al, 1984;Muramatsu and Imasato, 1987). The reason the SP2 conformation is more "rigid" should be explained by the fact that SP2 has at least two additional hydrophobic amino acid residues at the C-terminal region.…”

Section: Discussionmentioning

confidence: 99%

“…The enzyme from the midgut gland of a wreath shell, Turbo cornutus, has been purified and characterized (Muramatsu and Egawa, 1982;Muramatsu et al, 1984). The Turbo cornutus enzyme has two isoforms, referred to as SP1 and SP2, which are separable on SP-Sephadex A-50 column chromatography by application of subtle elution conditions with 70 mM phosphate buffer, pH 7.0, in purification steps.…”

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confidence: 99%

Primary structure of mannuronate lyases SP1 and SP2 fromTurbo cornutus and involvement of the hydrophobic C-terminal residues in the protein stability

et al. 1996

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The complete amino acid sequences of two isoforms, SP1 and SP2, of mannuronate lyase from a wreath shell, Turbo cornutus, were determined to elucidate amino acid residues responsible for causing the more stable protein conformation of SP2. The sequences of the two isoforms were identical except for two hydrophobic C-terminal amino acid residues of SP2, Ile and Leu, which were additionally attached to Thr of the C-terminal residue of SP1 (253 residues in total). The molecular weight of SP2 was calculated to be 28,912 from the amino acid sequence data. Two disulfide bond cross-linkages were found to be between 106 and 115 and between 145 and 150, and a partially buried single SH group was located at 236. A carbohydrate chain that consisted of 3 GlcNAc, 3 Fuc, and 1 Man was anchored on Asn-105 in a typical carbohydrate-binding motif of Asn-X-Ser. This is the first evidence of the primary structure of mannuronate lyase, and no significant homology of the amino acid sequence among other proteins was found. The C-terminal truncated SP2, which was produced by digestion with carboxypeptidase Y and corresponded structurally to SP1, showed a thermal stability identical to that of SP1. These results indicate that the higher stability of SP2 than SP1 arises from the presence of the C-terminal two hydrophobic amino acid residues.

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Purification and structural properties of an extracellular (1-4)-.beta.-D-mannuronan-specific alginate lyase from a marine bacterium

Romeo¹,

Preston²

1986

Biochemistry

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Physicochemical Characteristics and Conformational Features of Alginate Lyase Isozymes fromTurbo cornutus

Cited by 5 publications

References 6 publications

Crystal Structure of the Alginate (Poly α-l-guluronate) Lyase from Corynebacterium sp. at 1.2Å Resolution

Crystal Structure of the Alginate (Poly α-l-guluronate) Lyase from Corynebacterium sp. at 1.2Å Resolution

Primary structure of mannuronate lyases SP1 and SP2 fromTurbo cornutus and involvement of the hydrophobic C-terminal residues in the protein stability

Purification and structural properties of an extracellular (1-4)-.beta.-D-mannuronan-specific alginate lyase from a marine bacterium

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