Literature summary for 1.11.1.7 extracted from

Bernardes, A.; Textor, L.C.; Santos, J.C.; Cuadrado, N.H.; Kostetsky, E.Y.; Roig, M.G.; Bavro, V.N.; Muniz, J.R.; Shnyrov, V.L.; Polikarpov, I.
Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa (2015), Biochimie, 111, 58-69 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.6 A resolution. The enzyme displays a noncovalent homodimer assembly held together by a number of ionic and hydrophobic interactions and shows disulfide bonds Cys11-Cys91, Cys44-Cys49, Cys97-Cys299 and Cys176-Cys208	Trachycarpus fortunei

Organism

Organism	UniProt	Comment	Textmining
Trachycarpus fortunei	A0A0A0Y4H8	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	enzyme has five N-linked glycans at the positions of Asn8, Asn127, Asn185, Asn267 and Asn298, pointing away from the protein surface	Trachycarpus fortunei

Purification (Commentary)

Purification (Comment)	Organism
-	Trachycarpus fortunei

Reaction

Reaction	Comment	Organism	Reaction ID
2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O	ping-pong Bi-Bi reaction mechanism	Trachycarpus fortunei	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Trachycarpus fortunei	-

Subunits

Subunits	Comment	Organism
?	x * 50000, SDS-PAGE, x * 45000, calculated	Trachycarpus fortunei

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Release 2023.1 (January 2023)