Lyase Escherichia coli

Chen C-M, Q-Z Zhuang, Z Zhu, BL Wanner, CT Walsh (1990) Molecuar biology of carbon-phosphorus bond cleavage Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli. J Biol Chem 265 4461-4471. 

Hasslacher, M., Schall, M., Hayn, M. et al. (1996) Molecular cloning of the full-length cDNA of (5)-hydroxynitrile lyase from Hevea brasiliensis. Functional expression in Escherichia coli and Saccharomyces cerevisiae and identification of an active site residue. The Journal of Biological Chemistry, 271, 5884-5891. 

Knappe, J. and Sawers, G. (1990) A radical-chemical route to acetyl-CoA the anaerobically induced pyruvate formate-lyase system of Escherichia coli. FEMS Microbiology Reviews 75, 383-398. 

Escherichia coli [NiFe] hydrogenase 3 Membrane-associated component of the formate hydrogen lyase complex H2 production during fermentation H2 uptake under anaerobic conditions Anaerobiosis, carbon source limitation, phosphate limitation, molybdenum, nitrate, formate 7.8... 

FujuT, Maeda M, Mihara H, et al. 2000. Strnctnre of a NifS homologne X-ray strnc-ture analysis of CsdB, an Escherichia coli connterpart of mammalian selenocys-teine lyase. Biochemistry 39 1263-73. 

Zinoni E, Birkmann A, Stadtman TC, Bock A. 1986. Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli. Proc Natl Acad Sci USA 83 4650-4. 

J. Hughes, J. H. Lakey, M. A. Hughes, Production and characterization of a plant X hydroxynitrile lyase in Escherichia coli. Biotechnol. Bioeng. 1997, 53,... 

At present, there are some patents concerning the production of green notes by recombinant guava 13-hydroperoxide lyase expressed in Escherichia coli [70, 71] and Cucumis melo hydroperoxide lyase the latter yields a mixture of C6 and C9 compounds [72]. 

Kessler D, Herth W, Knappe J (1992) Ultrastructure and pyruvate formate-lyase radical quenching property of the multienzymatic ADHE protein of Escherichia coli. J Biol Chem 267 18073-18079... 

Y. Uchida, Y. Tuskada, and T. Sugimori, Purification and properties of W-acetylneuraminaie lyase from Escherichia coli, J. Biochem. 96 507 (1984). 

K. Aisaka, S. Tamura, Y. Arai, and T. Uwajimu, Hyperproduction of W-acetylneuraminate lyase by the gene-cloned strain of Escherichia coli, Biotechnol. Lett. 9 633 (1987). 

K. Aisaka, A. Igarashi, K. Yamagushi, and T. Uwajima, Purification, crystallisation and characterization of V-acety Incur animate lyase from Escherichia coli, Biochem. J. 276 541 (1991). 

T. Izard, M. C. Lawrence, R. L. Malby, G. G. Lilley, and P. M. Colman, The three-dimensional structure of 79-acetylneuraminate lyase from Escherichia coli, Structure 2 361 (1994). 

The bacterial formamidopyrimidine-DNA glycosylase (alias Fpg or MutM) is a bifunctional base-repair enzyme (DNA glycosylase/AP lyase) that removes a wide range of oxidized purines from oxidatively damaged DNA. The crystal structures of the Fpg (MutM) enzymes from Thermus thermophilus, Lactococcus lactis Escherichia coli Bacillus stearothermophilus and the sequence similar endonuclease VIII (Nei) from E. all share the same... 

Shen X, Woodgate R, Goodman ME. Lyase activities intrinsic to Escherichia coli polymerases IV and V. DNA Repair (Amst) 2005 4 1368-1373. 

Figure 1 Fermentation pathways of Escherichia coli. Gene symbols ackA, acetate kinase adhE, alcohol dehydrogenase fdh, formate dehydrogenase of FHL complex fhn, nitrate-inducible formate dehydrogenase hyd, hydrogenase 3 of FHL complex IdhA, NAD+-dependent D-(-)-lactate dehydrogenase pfl, pyruvate formate-lyase pta, phosphotransacetylase. FHL, formate hydrogenlyase. Redrawn from reference 29...

A biocatalytic enantioselective addition of ammonia to a C=C bond of an afl-unsaturated compound, namely fumaric acid, makes the manufacture of L-aspar-tic acid, l-27, possible [30], This L-amino acid represents an important intermediate for the production of the artificial sweetener aspartame. The biocatalytic production process, which is applied on an industrial scale by, e.g., Kyowa Hakko Ko-gyo and Tanabe Seiyaku, is based on the use of an aspartate ammonia lyase [E.C.4.3.1.1] [31]. As a biocatalyst, an immobilized L-aspartate ammonia lyase from Escherichia coli [32, 33] as well as Brevibacterium flavum whole-cell catalysts [32 a, 34] have been applied successfully. 

Fig. zi. 1 hree-dimensional structure of the sialate-pyruvate lyase from Escherichia coli. (top) Viewed down the (3-barrel axis from the carboxy-terminal end of this aldolase. The putative catalytic residue Lys-165 is shown in ball-and-stick representation, (bottom) Putative active site of Neu5Ac lyase showing the side chains of nine of the residues forming the surface of the pocket. Carbon atoms are white, oxygens black and nitrogens grey. From ref. [899] by permission of Current Biology Ltd., London. 

The enzyme methylaspartate ammonia lyase (P-methylaspartase, E.C. 4.3.1.2) is involved in the metabolism of branched pentanoic acids. The enzyme catalyzes the addition of ammonia to mesaconic acid (8) to yield i-tfireo-3-methylaspartate (9) as depicted in Scheme 12.6-3. The enzyme has been shown to be induced under anaerobic conditions in facultative anaerobes such as Citrobacter, Proteus, Escherichia coli and Enterobacter17, 81 and has been applied for the synthesis of 3-substituted (S)-aspartic acid derivatives, such as (2S,3S)-3-methylaspartic acid (9), (2S,3S)-3-ethylas-partic acid (11), and (2R,3S)-3-chloroaspartic acid (13) 7l In addition, a process for the preparation of dialkyl-(2S,3S)-3-ethylaspartates using methylaspartate ammonia lyase has been developed by Merck191. 

Imai, X, H. Globerman, J.M. Gertner, N. Kagawa, and M.R. Waterman (1993). Expression and purification of functional human 17a-hydroxy-lase/17,20-lyase (P450cl7) in Escherichia coli. Use of this system for study of a novel form of combined 17a-hydroxylase/17,20-lyase deficiency. J Biol. Chem. 268, 19681-19689. 

---