The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Alkaline Phosphatases: Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes
Open accessAbstract
Our knowledge of the structure and function of alkaline phosphatases has increased greatly in recent years. The crystal structure of the human placental isozyme has enabled us to probe salient features of the mammalian enzymes that differ from those of the bacterial enzymes. The availability of knockout mice deficient in each of the murine alkaline phosphatase isozymes has also given deep insights into their in vivo role. This has been particularly true for probing the biological role of bone alkaline phosphatase during skeletal mineralization. Due to space constraints this mini-review focuses exclusively on structural and functional features of mammalian alkaline phosphatases as identified by crystallography and probed by site-directed mutagenesis and kinetic analysis. An emphasis is also placed on the substrate specificity of alkaline phosphatases, their catalytic properties as phosphohydrolases as well as phosphodiesterases and their structural and functional relatedness to a large superfamily of enzymes that includes nucleotide pyrophosphatase/phosphodiesterase.
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Cites
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Self-citationHypophosphatasia and the Role of Alkaline Phosphatase in Skeletal Mineralization*
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Concerted Regulation of Inorganic Pyrophosphate and Osteopontin by Akp2, Enpp1, and Ank
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Self-citationMammalian Alkaline Phosphatases: From Biology to Applications in Medicine and Biotechnology
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Crystal Structure of Alkaline Phosphatase from Human Placenta at 1.8 Å Resolution
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Recent progresses in small-molecule enzymatic fluorescent probes for cancer imaging
Liu, H.-W., Chen, L., Xu, C., Li, Z., Zhang, H., Zhang, X.-B., & Tan, W. (2018) · Chemical Society Reviews · doi:10.1039/c7cs00862g · Cited by 948
Control of Vertebrate Skeletal Mineralization by Polyphosphates
Omelon, S., Georgiou, J., Henneman, Z. J., Wise, L. M., Sukhu, B., Hunt, T., Wynnyckyj, C., Holmyard, D., Bielecki, R., & Grynpas, M. D. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005634 · Cited by 216
Zhang, X., Chen, Y., He, H., Wang, S., Lei, Z., & Zhang, F. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202109728 · Cited by 176
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Metadata
- Authors
- Millán, J. L.
- Venue
- Purinergic Signalling
- Published
- 2006-06
- Volume
- 2
- Issue
- 2
- Pages
- 335-41
- ISSN
- 1573-9538 (ISSN-L)
- 1573-9546
- OpenAlex
- W2066052326
- Cited by
- 608
- References
- 30
- FWCI
- 5.45
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Millán, J. L. (2006). Alkaline Phosphatases: Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes. Purinergic Signalling. https://doi.org/10.1007/s11302-005-5435-6
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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