Capra et al., 2024 - Google Patents
Adapting an acyl CoA ligase from Metallosphaera sedula for lactam formation by structure-guided protein engineeringCapra et al., 2024
View HTML- Document ID
- 3496101589682890915
- Author
- Capra N
- Lelièvre C
- Touré O
- Fossey-Jouenne A
- Vergne-Vaxelaire C
- Janssen D
- Thunnissen A
- Zaparucha A
- Publication year
- Publication venue
- Frontiers in Catalysis
External Links
Snippet
The CoA ligase from Metallosphaera sedula (Ms ACL) can be used for the chemoenzymatic synthesis of amides from carboxylic acids. In this CoA-independent conversion, the enzyme catalyzes the adenylation of a carboxylic acid with the help of ATP, followed by the …
- 230000015572 biosynthetic process 0 title abstract description 9
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/12—Transferases (2.) transferring phosphorus containing groups, e.g. kinases (2.7)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1025—Acyltransferases (2.3)
- C12N9/1029—Acyltransferases (2.3) transferring groups other than amino-acyl groups (2.3.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/02—Preparation of oxygen-containing organic compounds containing a hydroxy group
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/40—Preparation of oxygen-containing organic compounds containing a carboxyl group including Peroxycarboxylic acids
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y401/00—Carbon-carbon lyases (4.1)
- C12Y401/01—Carboxy-lyases (4.1.1)
- C12Y401/01041—Methylmalonyl-CoA decarboxylase (4.1.1.41)
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Liu et al. | Dissection of malonyl-coenzyme A reductase of Chloroflexus aurantiacus results in enzyme activity improvement | |
| Rodríguez‐Mata et al. | Structure and Activity of NADPH‐Dependent Reductase Q1EQE0 from Streptomyces kanamyceticus, which Catalyses the R‐Selective Reduction of an Imine Substrate | |
| Ji et al. | Creation of bioorthogonal redox systems depending on nicotinamide flucytosine dinucleotide | |
| Hughes et al. | Enzymatic extender unit generation for in vitro polyketide synthase reactions: structural and func-tional showcasing of Streptomyces coelicolor MatB | |
| Sulzenbacher et al. | Crystal structure of E. coli alcohol dehydrogenase YqhD: evidence of a covalently modified NADP coenzyme | |
| Venkatesan et al. | Insights into mitochondrial fatty acid synthesis from the structure of heterotetrameric 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA dehydrogenase | |
| Sato et al. | Catalytic mechanism and endo-to-exo selectivity reversion of an octalin-forming natural Diels–Alderase | |
| Zhang et al. | Computational design of highly efficient thermostable MHET hydrolases and dual enzyme system for PET recycling | |
| Alonzo et al. | Structural basis of keto acid utilization in nonribosomal depsipeptide synthesis | |
| Pereira et al. | Structural and biochemical characterization of the early and late enzymes in the lignin β-aryl ether cleavage pathway from Sphingobium sp. SYK-6 | |
| Krawczyk et al. | Curvopeptin: A New Lanthionine‐Containing Class III Lantibiotic and its Co‐substrate Promiscuous Synthetase | |
| Javidpour et al. | Biochemical and structural studies of NADH-dependent FabG used to increase the bacterial production of fatty acids under anaerobic conditions | |
| Heckmann et al. | An (R)-selective transaminase from thermomyces stellatus: Stabilizing the tetrameric form | |
| Deng et al. | Structural and functional characterization of 4‐hydroxyphenylacetate 3‐hydroxylase from Escherichia coli | |
| Yu et al. | Engineering transketolase to accept both unnatural donor and acceptor substrates and produce α‐hydroxyketones | |
| Rossoni et al. | The putative mevalonate diphosphate decarboxylase from Picrophilus torridus is in reality a mevalonate-3-kinase with high potential for bioproduction of isobutene | |
| Bell et al. | Protein recognition in ferredoxin–P450 electron transfer in the class I CYP199A2 system from Rhodopseudomonas palustris | |
| Lassalle et al. | New insights into the mechanism of substrates trafficking in Glyoxylate/Hydroxypyruvate reductases | |
| Horita et al. | An engineered Old Yellow Enzyme that enables efficient synthesis of (4R, 6R)‐actinol in a one‐pot reduction system | |
| Kasaragod et al. | The isomerase and hydratase reaction mechanism of the crotonase active site of the multifunctional enzyme (type‐1), as deduced from structures of complexes with 3 S‐hydroxy‐acyl‐C o A | |
| Wang et al. | Identification of residues important for the activity of aldehyde-deformylating oxygenase through investigation into the structure-activity relationship | |
| Kurteva-Yaneva et al. | Structural basis of the stereospecificity of bacterial B12-dependent 2-hydroxyisobutyryl-CoA mutase | |
| Rahman et al. | An engineered variant of MECR reductase reveals indispensability of long-chain acyl-ACPs for mitochondrial respiration | |
| Xu et al. | Formaldehyde formation in the glycine cleavage system and its use for an aldolase-based biosynthesis of 1, 3-propanediol | |
| Wang et al. | Rational hinge engineering of carboxylic acid reductase from Mycobacterium smegmatis enhances its catalytic efficiency in biocatalysis |