Nothing Special   »   [go: up one dir, main page]

Lo et al., 2005 - Google Patents

Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement

Lo et al., 2005

Document ID
15453923783584767554
Author
Lo Y
Lin S
Shaw J
Liaw Y
Publication year
Publication venue
Biochemistry

External Links

Snippet

Escherichia coli thioesterase I/protease I/lysophospholipase L1 (TAP) is a multifunctional lysophospholipase and acyl-CoA thioesterase with a SGNH-hydrolase fold. The relationship between TAP's structure and its versatile substrate specificity, however, is unclear. Here, we …
Continue reading at pubs.acs.org (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/16Hydrolases (3) acting on ester bonds (3.1)
    • C12N9/18Carboxylic ester hydrolases (3.1.1)
    • C12N9/20Triglyceride splitting, e.g. by means of lipase
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/24Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/10Transferases (2.)
    • C12N9/1025Acyltransferases (2.3)
    • C12N9/1029Acyltransferases (2.3) transferring groups other than amino-acyl groups (2.3.1)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y301/00Hydrolases acting on ester bonds (3.1)

Similar Documents

Publication Publication Date Title
Grisewood et al. Computational redesign of acyl-ACP thioesterase with improved selectivity toward medium-chain-length fatty acids
Rivera-Colón et al. The structure of human GALNS reveals the molecular basis for mucopolysaccharidosis IV A
Lo et al. Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network
Glukhova et al. Structure and function of lysosomal phospholipase A2 and lecithin: cholesterol acyltransferase
Chen et al. Structure of bovine pancreatic cholesterol esterase at 1.6 Å: novel structural features involved in lipase activation
Bordes et al. Exploring the conformational states and rearrangements of Yarrowia lipolytica lipase
Lo et al. Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement
Yaacob et al. The role of solvent-accessible Leu-208 of cold-active Pseudomonas fluorescens strain AMS8 lipase in interfacial activation, substrate accessibility and low-molecular weight esterification in the presence of toluene
Cao et al. The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis
Ingram-Smith et al. Characterization of the acyl substrate binding pocket of acetyl-CoA synthetase
Herrgård et al. Role of an electrostatic network of residues in the enzymatic action of the Rhizomucor miehei lipase family
Latip et al. The effect of N-terminal domain removal towards the biochemical and structural features of a thermotolerant lipase from an antarctic Pseudomonas sp. strain AMS3
Shao et al. Biochemical characterization of a carboxylesterase from the archaeon Pyrobaculum sp. 1860 and a rational explanation of its substrate specificity and thermostability
Miller et al. Structural features and domain movements controlling substrate binding and cofactor specificity in class II HMG-CoA reductase
Jiang et al. Improving the thermostability of Rhizopus chinensis lipase through site-directed mutagenesis based on B-factor analysis
Sayer et al. The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis reveals an open active site due to a minimal ‘cap’domain
Wang et al. Propeptide in Rhizopus chinensis lipase: new insights into its mechanism of activity and substrate selectivity by computational design
Wang et al. Catalytic site flexibility facilitates the substrate and catalytic promiscuity of Vibrio dual lipase/transferase
McKary et al. Structural basis for the strict substrate selectivity of the mycobacterial hydrolase LipW
Fernandez-Lopez et al. Enhancing the hydrolytic activity of a lipase towards larger triglycerides through lid domain engineering
Ishak et al. Ion-pair interaction and hydrogen bonds as main features of protein thermostability in mutated T1 recombinant lipase originating from Geobacillus zalihae
Rodríguez-Salarichs et al. Versatile lipases from the candida rugosa-like family: A mechanistic insight using computational approaches
Masomian et al. A novel method of affinity tag cleavage in the purification of a recombinant thermostable lipase from Aneurinibacillus thermoaerophilus strain HZ
Xu et al. Biochemical properties and structure analysis of a DAG-Like lipase from Malassezia globosa
Bannitz-Fernandes et al. Non-mammalian Prdx6 enzymes (proteins with 1-Cys Prdx mechanism) display PLA2 activity similar to the human orthologue