Manganese-dependent peroxidase from Phanerochaete chrysosporium. Primary structure deduced from cDNA sequence.

E. A. Pease, A. Andrawis, Ming Tien

Research output: Contribution to journalArticle

96 Citations (Scopus)

Abstract

A cDNA clone encoding a manganese-dependent peroxidase from the filamentous fungus Phanerochaete chrysosporium was isolated and characterized. The clone, lambda MP-1, was isolated by screening a lambda gt11 expression library with polyclonal antibodies raised against a purified manganese-dependent peroxidase (isozyme H4, pI 4.5). The lambda MP-1 cDNA sequence predicts a mature protein containing 358 amino acids with a molecular weight of 37,711 preceded by a leader peptide of 24 amino acid residues. The N-terminal amino acid sequence of a purified manganese-dependent peroxidase (H4) corresponds to the sequence deduced from the cDNA. Some homology (58% in nucleotide sequence and 65% in amino acid sequence) is observed between the manganese-dependent peroxidase and lignin peroxidase isozyme H8. The highest degree of similarity is observed near the enzyme active site. Residues essential for peroxidase activity, the distal and proximal histidines, can be identified in the amino acid sequence. Near these residues, homology is also observed with several other peroxidases. Northern blot analysis of poly(A)+ RNA from nitrogen-limited P. chrysosporium cultures indicates that the level of messenger RNA correlates with expression of the enzyme and its activity. This is consistent with the regulation of the enzyme being at the level of transcription.

Original languageEnglish (US)
Pages (from-to)13531-13535
Number of pages5
JournalThe Journal of biological chemistry
Volume264
Issue number23
StatePublished - Jan 1 1989

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manganese peroxidase
Phanerochaete
Complementary DNA
Amino Acids
Amino Acid Sequence
Isoenzymes
Enzymes
Clone Cells
Peroxidases
Messenger RNA
Protein Sorting Signals
Histidine
Northern Blotting
Peroxidase
Transcription
Catalytic Domain
Fungi
Nitrogen
Molecular Weight
Screening

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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title = "Manganese-dependent peroxidase from Phanerochaete chrysosporium. Primary structure deduced from cDNA sequence.",
abstract = "A cDNA clone encoding a manganese-dependent peroxidase from the filamentous fungus Phanerochaete chrysosporium was isolated and characterized. The clone, lambda MP-1, was isolated by screening a lambda gt11 expression library with polyclonal antibodies raised against a purified manganese-dependent peroxidase (isozyme H4, pI 4.5). The lambda MP-1 cDNA sequence predicts a mature protein containing 358 amino acids with a molecular weight of 37,711 preceded by a leader peptide of 24 amino acid residues. The N-terminal amino acid sequence of a purified manganese-dependent peroxidase (H4) corresponds to the sequence deduced from the cDNA. Some homology (58{\%} in nucleotide sequence and 65{\%} in amino acid sequence) is observed between the manganese-dependent peroxidase and lignin peroxidase isozyme H8. The highest degree of similarity is observed near the enzyme active site. Residues essential for peroxidase activity, the distal and proximal histidines, can be identified in the amino acid sequence. Near these residues, homology is also observed with several other peroxidases. Northern blot analysis of poly(A)+ RNA from nitrogen-limited P. chrysosporium cultures indicates that the level of messenger RNA correlates with expression of the enzyme and its activity. This is consistent with the regulation of the enzyme being at the level of transcription.",
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Manganese-dependent peroxidase from Phanerochaete chrysosporium. Primary structure deduced from cDNA sequence. / Pease, E. A.; Andrawis, A.; Tien, Ming.

In: The Journal of biological chemistry, Vol. 264, No. 23, 01.01.1989, p. 13531-13535.

Research output: Contribution to journalArticle

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N2 - A cDNA clone encoding a manganese-dependent peroxidase from the filamentous fungus Phanerochaete chrysosporium was isolated and characterized. The clone, lambda MP-1, was isolated by screening a lambda gt11 expression library with polyclonal antibodies raised against a purified manganese-dependent peroxidase (isozyme H4, pI 4.5). The lambda MP-1 cDNA sequence predicts a mature protein containing 358 amino acids with a molecular weight of 37,711 preceded by a leader peptide of 24 amino acid residues. The N-terminal amino acid sequence of a purified manganese-dependent peroxidase (H4) corresponds to the sequence deduced from the cDNA. Some homology (58% in nucleotide sequence and 65% in amino acid sequence) is observed between the manganese-dependent peroxidase and lignin peroxidase isozyme H8. The highest degree of similarity is observed near the enzyme active site. Residues essential for peroxidase activity, the distal and proximal histidines, can be identified in the amino acid sequence. Near these residues, homology is also observed with several other peroxidases. Northern blot analysis of poly(A)+ RNA from nitrogen-limited P. chrysosporium cultures indicates that the level of messenger RNA correlates with expression of the enzyme and its activity. This is consistent with the regulation of the enzyme being at the level of transcription.

AB - A cDNA clone encoding a manganese-dependent peroxidase from the filamentous fungus Phanerochaete chrysosporium was isolated and characterized. The clone, lambda MP-1, was isolated by screening a lambda gt11 expression library with polyclonal antibodies raised against a purified manganese-dependent peroxidase (isozyme H4, pI 4.5). The lambda MP-1 cDNA sequence predicts a mature protein containing 358 amino acids with a molecular weight of 37,711 preceded by a leader peptide of 24 amino acid residues. The N-terminal amino acid sequence of a purified manganese-dependent peroxidase (H4) corresponds to the sequence deduced from the cDNA. Some homology (58% in nucleotide sequence and 65% in amino acid sequence) is observed between the manganese-dependent peroxidase and lignin peroxidase isozyme H8. The highest degree of similarity is observed near the enzyme active site. Residues essential for peroxidase activity, the distal and proximal histidines, can be identified in the amino acid sequence. Near these residues, homology is also observed with several other peroxidases. Northern blot analysis of poly(A)+ RNA from nitrogen-limited P. chrysosporium cultures indicates that the level of messenger RNA correlates with expression of the enzyme and its activity. This is consistent with the regulation of the enzyme being at the level of transcription.

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