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Articles by Chenghai Sun
Direct asymmetric synthesis of β-branched aromatic α-amino acids using engineered phenylalanine ammonia lyases - Nature Communications
Abstract β-Branched aromatic α-amino acids are valuable building blocks in natural products and pharmaceutically active compounds. However, their chemical or enzymatic synthesis is challenging due to the presence of two stereocenters. We design phenylalanine ammonia lyases (PAL) variants for the direct asymmetric synthesis of β-branched aromatic α-amino acids.
Systematic Analysis of the MIO‐forming Residues of Aromatic Ammonia Lyases
Introduction The group of 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO)-dependent enzymes is a large family which includes phenylalanine ammonia lyase (PAL, EC 4.3.1.24), tyrosine ammonia lyases (TAL, EC 4.3.1.23), tyrosine/phenylalanine ammonia lyases (PTAL, EC 4.3.1.25), histidine ammonia lyases (HAL, EC 4.3.1.3), as well as tyrosine 2,3-aminomutases (TAM, EC 5.4.3.6) and phenylalanine 2,3-aminomutases (PAM, EC 5.4.3.10).
Systematic Analysis of the MIO‐forming Residues of Aromatic Ammonia Lyases
Supporting Information As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors.
Exploring the Substrate Switch Motif of Aromatic Ammonia Lyases
Supporting Information As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors.
Engineering the Substrate Specificity of a P450 Dimerase Enables the Collective Biosynthesis of Heterodimeric Tryptophan‐Containing Diketopiperazines
Graphical Abstract The biosynthesis of heterodimeric tryptophan-containing diketopiperazines (HTDKPs) is restricted by the limited substrate scopes of the HTDKP-forming P450 dimerases. Engineering of three important residues (F387, F388, and E73) in NasF5053 significantly expanded its substrate specificity and enabled the collective biosynthesis of at least 93 HTDKPs. Abstract Heterodimeric tryptophan-containing diketopiperazines (HTDKPs) are an important class of bioactive secondary metabolites.
Biosynthesis of plant tetrahydroisoquinoline alkaloids through an imine reductase route
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Structural Basis of a Broadly Selective Acyltransferase from the Polyketide Synthase of Splenocin
Polyketides are a large family of pharmaceutically important natural products, and the structural modification of their scaffolds is significant for drug development. Herein, we report one apo- and two complex structures (with a pentynylmalonyl and benzylmalonyl, respectively) of the broadly selective acyltransferase (AT) from the splenocin polyketide synthase.
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