Structural and Kinetic Analysis of Bacillus subtilis N-Acetylglucosaminidase 
Reveals a Unique Asp-His Dyad Mechanism

Litzinger, S.; Fischer, S.; Polzer, Patrick; Diederichs, K.; Welte, W.; Mayer, C.

doi:10.1074/jbc.M110.131037

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Structural and Kinetic Analysis of Bacillus subtilis N-Acetylglucosaminidase Reveals a Unique Asp-His Dyad Mechanism

Litzinger, S., Fischer, S., Polzer, P., Diederichs, K., Welte, W., & Mayer, C. (2010). Structural and Kinetic Analysis of Bacillus subtilis N-Acetylglucosaminidase Reveals a Unique Asp-His Dyad Mechanism. Journal of Biological Chemistry, 285(46), 35675-35684. doi:10.1074/jbc.M110.131037.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-000F-AF2C-0 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-000F-AF2D-E

Genre: Journal Article

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Creators:
Litzinger, S., Author
Fischer, S., Author
Polzer, Patrick¹, Author
Diederichs, K., Author
Welte, W., Author
Mayer, C., Author

Affiliations:
1Laboratory for Attosecond Physics, Max Planck Institute of Quantum Optics, Max Planck Society, ou_1445564

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Language(s): eng - English

Dates: Date issued: 2010-11-12

Publication Status: Issued

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Rev. Type: Peer

Identifiers: eDoc: 522456
URI: http://www.jbc.org/content/285/46/35675.abstract?sid=7a0d3b7e-b003-4bd1-a2b7-2ddf824c0227
DOI: 10.1074/jbc.M110.131037
Other: 4038

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Title: Journal of Biological Chemistry

Source Genre: Journal

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Pages: - Volume / Issue: 285 (46) Sequence Number: - Start / End Page: 35675 - 35684 Identifier: -