Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell
Abstract
Lysyl oxidase (LO) plays a critical role in the formation and repair of the extracellular matrix (ECM) by oxidizing lysine residues in elastin and collagen, thereby initiating the formation of covalent crosslinkages which stabilize these fibrous proteins. Its catalytic activity depends upon both its copper cofactor and a unique carbonyl cofactor and has been shown to extend to a variety of basic globular proteins, including histone H1. Although the three‐dimensional structure of LO has yet to be determined, the present treatise offers hypotheses based upon its primary sequence, which may underlie the prominent electrostatic component of its unusual substrate specificity as well as the catalysis‐suppressing function of the propeptide domain of prolysyl oxidase. Recent studies have demonstrated that LO appears to function within the cell in a manner, which strongly modifies cellular activity. Newly discovered LO‐like proteins also likely play unique roles in biology. © 2002 Wiley‐Liss, Inc.
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LOXL3 encodes a copper-dependent amine oxidase required for the formation of lysine-derived cross-links of COLLs and ELN fibrils.
“LOXL3 encodes a copper-dependent amine oxidase required for the formation of lysine-derived cross-links of COLLs and ELN fibrils [37].”
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- Authors
- Kagan, H. M., & Li, W.
- Affiliations
- Boston University (US)
- Corresponding author
- Kagan, Herbert M.
- ORCID
- Li, Wande
- Venue
- Journal of Cellular Biochemistry
- Publisher
- Wiley
- Published
- 2002-11-27
- Volume
- 88
- Issue
- 4
- Pages
- 660-672
- ISSN
- 0730-2312 (ISSN-L)
- 1097-4644
- OpenAlex
- W2100044667
- Cited by
- 954
- References
- 56
- Citations by year
- 2026: 29 · 2025: 39 · 2024: 38 · 2023: 48 · 2022: 42 · 2021: 36 · 2020: 46 · 2019: 52 · 2018: 51 · 2017: 47 · 2016: 60 · 2015: 42 · 2014: 43 · 2013: 48 · 2012: 59
- FWCI
- 0.99
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cellular Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r37ar018880-22)
- National Heart, Lung, and Blood Institute (HL13262, P01HL013262)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R37-AR-18880)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- lysyl oxidase, extracellular matrix, elastin, collagen, lysine oxidation, covalent cross-linking, copper cofactor, histone H1, substrate specificity, protein structure
- MeSH terms
- Amino Acid Oxidoreductases, Amino Acid Sequence, Animals, Catalysis, Cattle, Collagen, Elastin, Extracellular Matrix, Forecasting, Humans, Protein-Lysine 6-Oxidase, Molecular Sequence Data, Structure-Activity Relationship, Substrate Specificity, Tumor Suppressor Proteins, Myocytes, Smooth Muscle, Rats
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