Amino acid sequence determination of the blocked N‐terminal tryptic peptide of <i>Neurospora</i> tyrosinase by mass spectrometry

Nau, Heinz; Lerch, Konrad; Witte, Ludger

doi:10.1016/0014-5793(77)80384-0

Cited by 10 publications

(1 citation statement)

References 18 publications

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“…Cleavage of the protein with cyanogen bromide yielded four major fragments and one minor overlap peptide due to incomplete cleavage of a methionyl-threonyl bond. Automatic sequence analysis of the cyanogen bromide fragments CB1, CB2, and CB4 allowed an unambiguous sequence determination of the first 25 to 30 residues, whereas CBS turned out to be blocked by an acetyl group, previously identified by mass spectrometry (21). The amino-terminal sequence of the overlap fragment CB2-4 was found to be identical with the one of CB4 and because fragment CB2 lacks homoserine the four primary cyanogen bromide fragments were aligned in the order CB3-CB1-CB4-CB2 (Fig.…”

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confidence: 96%

Amino acid sequence of tyrosinase from Neurospora crassa.

Lerch¹

1978

Proc. Natl. Acad. Sci. U.S.A.

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The amino-acid sequence of tyrosinase from Neurospora crassa (monophenol,dihydroxyphenylalanine:oxygen oxidoreductase, EC 1.14.18.1) is reported. This copper-containing oxidase consists of a single polypeptide chain of 407 amino acids. The primary structure was determined by automated and manual sequence analysis on fragments produced by cleavage with cyanogen bromide and on peptides obtained by digestion with trypsin, pepsin, thermolysin, or chymotrypsin. The amino terminus of the protein is acetylated and the single cysteinyl residue 96 is covalently linked via a thioether bridge to histidyl residue 94. The formation and the possible role of this unusual structure in Neurospora tyrosinase is discussed. Dye-sensitized photooxidation of apotyrosinase and active-site-directed inactivation of the native enzyme indicate the possible involvement of histidyl residues 188, 192, 289, and 305 or 306 as ligands to the active-site copper as well as in the catalytic mechanism of this monooxygenase.

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mentioning

confidence: 96%

Amino acid sequence of tyrosinase from Neurospora crassa.

Lerch¹

1978

Proc. Natl. Acad. Sci. U.S.A.

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Neurospora tyrosinase: structural, spectroscopic and catalytic properties

1983

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Tyrosinase is a copper containing monooxygenase catalyzing the formation of melanin pigments and other polyphenolic compounds from various phenols. This review deals with the recent progress on the molecular structure of the enzyme from Neurospora crassa and the unique features of the binuclear active site copper complex involved in the activation of molecular oxygen and the binding of substrates. The results of the spectroscopic properties of Neurospora tyrosinase will also be discussed in the light of the structural similarity of the copper complex in the oxygen binding hemocyanins.

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