The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Cobalt proteins
Abstract
In the form of vitamin B 12, cobalt plays a number of crucial roles in many biological functions. However, recent studies have provided information on the biochemistry and bioinorganic chemistry of several proteins containing cobalt in a form other than that in the corrin ring of vitamin B 12. To date, eight noncorrin‐cobalt‐containing enzymes (methionine aminopeptidase, prolidase, nitrile hydratase, glucose isomerase, methylmalonyl‐CoA carboxytransferase, aldehyde decarbonylase, lysine‐2,3‐aminomutase, and bromoperoxidase) have been isolated and characterized. A cobalt transporter is involved in the metallocenter biosynthesis of the host cobalt‐containing enzyme, nitrile hydratase. Understanding the differences between cobalt and nickel transporters might lead to drug development for gastritis and peptic ulceration.
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Cites
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Self-citationN-Terminal processing: the methionine aminopeptidase and Nα-acetyl transferase families
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Cited by
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Fluorescent, MRI, and colorimetric chemical sensors for the first-row d-block metal ions
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Structure and function of the methionine aminopeptidases
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Metadata
- Authors
- Kobayashi, M., & Shimizu, S.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1999-03-19
- Volume
- 261
- Issue
- 1
- Pages
- 1-9
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W3192366276
- Cited by
- 441
- References
- 34
- FWCI
- 16.17
- Type
- journal article
- Language
- en
- Open access
- closed
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