Disulfide bonds and glycosylation in fungal peroxidases
(1995) In European Journal of Biochemistry 227(1-2). p.270-276- Abstract
- Four conserved disulfide bonds and N-linked and O-linked glycans of extracellular fungal peroxidases have been identified from studies of a lignin and a manganese peroxidase from Trametes versicolor, and from Coprinus cinereus peroxidase (CIP) and recombinant C. cinereus peroxidase (rCIP) expressed in Aspergillus oryzae. The eight cysteine residues are linked 1-3, 2-7, 4-5 and 6-8, and are located differently from the four conserved disulfide bridges present in the homologous plant peroxidases. CIP and rCIP were identical in their, glycosylation pattern, although the extent of glycan chain heterogeneity depended on the fermentation batch. CIP and rCIP have one N-linked glycan composed only of GlcNAc and Man at residue Asn142, and two... (More)
- Four conserved disulfide bonds and N-linked and O-linked glycans of extracellular fungal peroxidases have been identified from studies of a lignin and a manganese peroxidase from Trametes versicolor, and from Coprinus cinereus peroxidase (CIP) and recombinant C. cinereus peroxidase (rCIP) expressed in Aspergillus oryzae. The eight cysteine residues are linked 1-3, 2-7, 4-5 and 6-8, and are located differently from the four conserved disulfide bridges present in the homologous plant peroxidases. CIP and rCIP were identical in their, glycosylation pattern, although the extent of glycan chain heterogeneity depended on the fermentation batch. CIP and rCIP have one N-linked glycan composed only of GlcNAc and Man at residue Asn142, and two O-linked glycans near the C-terminus. The major glycoform consists of single Man residues at Thr331 and at Ser338. T. versicolor lignin isoperoxidase TvLP10 contains a single N-linked glycan composed of (GlcNAc)(2)Man(5) bound to Asn103, whereas (GlcNAc)(2)Man(3) was found in T. versicolor manganese isoperoxidase TvMP2 at the same position. In addition, mass spectrometry of the C-terminal peptide of TvMP2 indicated the presence of five Man residues in O-linked glycans. No phosphate was found in these fungal peroxidases. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/127053
- author
- Limongi, P ; Kjalke, M ; Vind, J ; Tams, J W ; Johansson, T and Welinder, K G
- publishing date
- 1995
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- AMINO ACID SEQUENCE, POSTTRANSLATIONAL MODIFICATION, RECOMBINANT PEROXIDASE, GLYCANS, PEROXIDASE
- in
- European Journal of Biochemistry
- volume
- 227
- issue
- 1-2
- pages
- 270 - 276
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:0028883288
- ISSN
- 0014-2956
- DOI
- 10.1111/j.1432-1033.1995.tb20384.x
- language
- English
- LU publication?
- no
- id
- 44bbdebe-0a80-490f-88b1-6d263b2c10f9 (old id 127053)
- date added to LUP
- 2016-04-01 16:24:28
- date last changed
- 2021-01-03 09:49:12
@article{44bbdebe-0a80-490f-88b1-6d263b2c10f9,
abstract = {{Four conserved disulfide bonds and N-linked and O-linked glycans of extracellular fungal peroxidases have been identified from studies of a lignin and a manganese peroxidase from Trametes versicolor, and from Coprinus cinereus peroxidase (CIP) and recombinant C. cinereus peroxidase (rCIP) expressed in Aspergillus oryzae. The eight cysteine residues are linked 1-3, 2-7, 4-5 and 6-8, and are located differently from the four conserved disulfide bridges present in the homologous plant peroxidases. CIP and rCIP were identical in their, glycosylation pattern, although the extent of glycan chain heterogeneity depended on the fermentation batch. CIP and rCIP have one N-linked glycan composed only of GlcNAc and Man at residue Asn142, and two O-linked glycans near the C-terminus. The major glycoform consists of single Man residues at Thr331 and at Ser338. T. versicolor lignin isoperoxidase TvLP10 contains a single N-linked glycan composed of (GlcNAc)(2)Man(5) bound to Asn103, whereas (GlcNAc)(2)Man(3) was found in T. versicolor manganese isoperoxidase TvMP2 at the same position. In addition, mass spectrometry of the C-terminal peptide of TvMP2 indicated the presence of five Man residues in O-linked glycans. No phosphate was found in these fungal peroxidases.}},
author = {{Limongi, P and Kjalke, M and Vind, J and Tams, J W and Johansson, T and Welinder, K G}},
issn = {{0014-2956}},
keywords = {{AMINO ACID SEQUENCE; POSTTRANSLATIONAL MODIFICATION; RECOMBINANT PEROXIDASE; GLYCANS; PEROXIDASE}},
language = {{eng}},
number = {{1-2}},
pages = {{270--276}},
publisher = {{Wiley-Blackwell}},
series = {{European Journal of Biochemistry}},
title = {{Disulfide bonds and glycosylation in fungal peroxidases}},
url = {{http://dx.doi.org/10.1111/j.1432-1033.1995.tb20384.x}},
doi = {{10.1111/j.1432-1033.1995.tb20384.x}},
volume = {{227}},
year = {{1995}},
}