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  ENHANCEMENT OF THE ENANTIOSELECTIVITY OF PENICILLIN-G ACYLASE FROM ESCHERICHIA-COLI BY SUBSTRATE TUNING

POHL, T., & Waldmann, H. (1995). ENHANCEMENT OF THE ENANTIOSELECTIVITY OF PENICILLIN-G ACYLASE FROM ESCHERICHIA-COLI BY SUBSTRATE TUNING. TETRAHEDRON LETTERS, 36(17), 2963-2966. doi:10.1016/0040-4039(95)00440-N.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0014-729A-9 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0014-9A97-2
Genre: Journal Article

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 Creators:
POHL, T1, Author
Waldmann, Herbert2, Author           
Affiliations:
1external, ou_persistent22              
2Abt. IV: Chemische Biologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753290              

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Free keywords: PEN-G ACYLASE; CATALYZED-HYDROLYSIS; PHENYLACETATE ESTERS; RESOLUTION; ASPARTAME
 Abstract: The efficiency of penicillin G acylase catalyzed transformations is enhanced significantly with respect to reaction velocity, and in particular, stereoselectivity by appropriate ''substrate tuning'', i.e. by the introduction of a nitrogen atom into the part of the substrates which is recognized by the enzyme.

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Language(s): eng - English
 Dates: 1995
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: A1995QV35800019
DOI: 10.1016/0040-4039(95)00440-N
 Degree: -

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Title: TETRAHEDRON LETTERS
Source Genre: Journal
 Creator(s):
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Publ. Info: KIDLINGTON, OXFORD : PERGAMON-ELSEVIER SCIENCE
Pages: - Volume / Issue: 36 (17) Sequence Number: - Start / End Page: 2963 - 2966 Identifier: ISSN: 0040-4039