TY - JOUR
T1 - Characterization of two lignin peroxidase clones from Phanerochaete chrysosporium
AU - Andrawis, Andrawis
AU - Pease, Elizabeth A.
AU - Kuan, I. ching
AU - Holzbaur, Erika
AU - Tien, Ming
N1 - Funding Information:
This work was supported in part by United State Department of Energy Grant DE-FGO2-87ERl36990. Andrawis Andmwis is a recipient of a United States-Israel Binational Agricultuml Research and Development Postdoctorate Fellowship. Tbe pmsent address for E&a Holzbaur is~ Worcester Foundation for Experimental Biology, 222 Maple Avenue, Shrewsbury, MA 01545. Ming Tien is a recipient of a Presidential Young Investigator Award from the National Science Foundation. Oligonucleotides were synthesized by Don Bryant at Pennsylvania State University. The N-terminu amino acid sequences of H2 and H9 were kindly provided by Steve Aust at Utah State University. The N-terminus sequences of H6 and HlO were provided by John Pierce of E. I. DuPont de Nemouts and Co.
PY - 1989/7/31
Y1 - 1989/7/31
N2 - Two cDNA clones encoding lignin peroxidase isozymes from Phanerochaete chrysosporium have been isolated and characterized. One of the clones, λML-4, encodes isozyme H8 as does the previously reported clone λML-1 [Tien, M. and Tu, C.-P.D. Nature 326 (1987) 520-523; 328, 742]. Our data are consistent with λML-1 and λML-4 being allelic variants. The other clone, λML-5, encodes a homologous isozyme. We have also isolated the genomic clone corresponding to λML-4 cDNA. Conserved residues thought to be essential for peroxidase function were identified in the predicted amino acid sequences of both cDNA clones. Northern blot analyses indicate that these isozymes are expressed during secondary metabolism, appearing on day 4 of growth and increasing on days 5 and 6.
AB - Two cDNA clones encoding lignin peroxidase isozymes from Phanerochaete chrysosporium have been isolated and characterized. One of the clones, λML-4, encodes isozyme H8 as does the previously reported clone λML-1 [Tien, M. and Tu, C.-P.D. Nature 326 (1987) 520-523; 328, 742]. Our data are consistent with λML-1 and λML-4 being allelic variants. The other clone, λML-5, encodes a homologous isozyme. We have also isolated the genomic clone corresponding to λML-4 cDNA. Conserved residues thought to be essential for peroxidase function were identified in the predicted amino acid sequences of both cDNA clones. Northern blot analyses indicate that these isozymes are expressed during secondary metabolism, appearing on day 4 of growth and increasing on days 5 and 6.
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U2 - 10.1016/0006-291X(89)92363-2
DO - 10.1016/0006-291X(89)92363-2
M3 - Article
C2 - 2474293
AN - SCOPUS:0024309247
SN - 0006-291X
VL - 162
SP - 673
EP - 680
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -