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The Enzymatic Cleavage of the Carbon-Nitrogen Bond in 3α,7α,12α-Trihydroxy-5β-cholan-24-oylglycine
Open accessAbstract
Abstract An enzyme from Clostridium perfringens capable of catalyzing the cleavage of the carbon-nitrogen bond in 3α,7α, 12α-trihydroxy-5β-cholan-24-oylglycine is described. The 15-fold purified enzyme hydrolyzes 3α,12α-dihydroxy-5β-cholan-24-oylglycine at a slightly faster rate than glycocholic acid. The Km for glycocholic acid in 0.01 m acetate buffer, pH 5.6, is approximately 8.0 x 10-3 m. 3,7,12-Triketo-5β-cholan-24-oylglycine, a substrate analogue, and 3,7,12-triketo-5β-cholanoic acid are enzyme inhibitors. Cholic acid exhibited competitive product inhibition in the present system. The enzyme is inhibited by sulfhydryl group inhibitors.
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Cited by
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Isolauri, E., Kaila, M., Mykkänen, H., Ling, W. H., & Salminen, S. (1994) · Digestive Diseases and Sciences · doi:10.1007/bf02087695 · Cited by 269
Grill, J., Schneider, F., Crociani, J., & Ballongue, J. (1995) · Applied and Environmental Microbiology · doi:10.1128/aem.61.7.2577-2582.1995 · Cited by 105
Bile salt hydrolases: Structure and function, substrate preference, and inhibitor development
Dong, Z., & Lee, B. H. (2018) · Protein Science · doi:10.1002/pro.3484 · Cited by 92
Metadata
- Authors
- Nair, P. P., Gordon, M., & Reback, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1967-01
- Volume
- 242
- Issue
- 1
- Pages
- 7-11
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1584619265
- Cited by
- 175
- References
- 0
- FWCI
- 3.54
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: The Enzymatic Cleavage of the Carbon-Nitrogen Bond in 3α,7α,12α-Trihydroxy-5β-cholan-24-oylglycine. https://app.cochat.ai/papers/10.1016/s0021-9258(18)96311-8
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- Nair, P. P., Gordon, M., & Reback, J. (1967). The Enzymatic Cleavage of the Carbon-Nitrogen Bond in 3α,7α,12α-Trihydroxy-5β-cholan-24-oylglycine. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)96311-8
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