Structure of Yak Lactoperoxidase at 1.55 Å Resolution.
Amino Acids
/ chemistry
Ammonium Compounds
/ chemistry
Animals
Binding Sites
Cattle
Colostrum
/ chemistry
Crystallization
Crystallography, X-Ray
Female
Gene Expression
Heme
/ chemistry
Hydrogen Peroxide
/ chemistry
Lactoperoxidase
/ chemistry
Models, Molecular
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Substrate Specificity
Conformation
Crystal structure
Iodide ion
Lactoperoxidase
Substrate binding channel
Journal
The protein journal
ISSN: 1875-8355
Titre abrégé: Protein J
Pays: Netherlands
ID NLM: 101212092
Informations de publication
Date de publication:
02 2021
02 2021
Historique:
accepted:
20
12
2020
pubmed:
4
1
2021
medline:
25
5
2021
entrez:
3
1
2021
Statut:
ppublish
Résumé
Lactoperoxidase (LPO) is a heme containing oxido-reductase enzyme. It is secreted from mammary, salivary, lachrymal and mucosal glands. It catalyses the conversion of thiocyanate into hypothiocyanate and halides into hypohalides. LPO belongs to the superfamily of mammalian heme peroxidases which also includes myeloperoxidase (MPO), eosinophil peroxidase (EPO) and thyroid peroxidase (TPO). The heme prosthetic group is covalently linked in LPO through two ester bonds involving conserved residues Glu258 and Asp108. It was isolated from colostrum of yak (Bos grunniens), purified to homogeneity and crystallized using ammonium iodide as a precipitating agent. The crystals belonged to monoclinic space group P2
Identifiants
pubmed: 33389415
doi: 10.1007/s10930-020-09957-2
pii: 10.1007/s10930-020-09957-2
doi:
Substances chimiques
Amino Acids
0
Ammonium Compounds
0
Heme
42VZT0U6YR
Hydrogen Peroxide
BBX060AN9V
Lactoperoxidase
EC 1.11.1.-
ammonium iodide
OZ8F027LDH
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
8-18Références
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