Decarboxylases lysine decarboxylase

Kikuchi Y, H Kojima, T Tanaka, Y Takatsuka, Y Kamio (1997) Characterization of a second lysine decarboxylase isolated from Escherichia coli. J Bacterial 179 4486-4492. 

Lemonnier M, D Lane (1998) Expession of the second lysine decarboxylase gene of Escherichia coli. Microbiology (UK) 144 751-761. 

LYSINE 2,3-AMINOMUTASE LYSINE 6-AMINOTRANSFERASE LYSINE DECARBOXYLASE... 

KYNURENINE AMINOTRANSFERASE LEUCINE AMINOTRANSFERASE LYSINE 2,3-AMINOMUTASE LYSINE 6-AMINOTRANSFERASE LYSINE DECARBOXYLASE METHIONINE y-LYASE ORNITHINE AMINOTRANSFERASE PHENYLALANINE DECARBOXYLASE PHOSPHATIDYLSERINE DECARBOXYLASE... 

The lysine sensor reported by Karube et al. was a micro-C02 sensor containing immobilized L-lysine decarboxylase (LDC, Fig. 3.18.C). L-lysine catalysed the following reaction... 

In related work, a-difluoromethyllysine (DFML) (111) was synthesized and shown to be a potent irreversible inhibitor of lysine decarboxylase, responsible for the biosynthesis of cadaverine. This analogue has been examined as a potential drug for the treatment of certain mycoplasmic infections176. 

The enzyme, i.e. lysine decarboxylase, that is required for the conversion of lysine into cadaverine, and thus the first step of alkaloid biosynthesis, has been isolated from chloroplasts of L. polyphyllus,28 Like the majority of amino-acid decarboxylases, this enzyme is dependent on pyridoxal 5 phosphate. Its activity was found not to be affected by the presence or absence of quinolizidine alkaloids. Control of the enzyme by simple product feedback inhibition therefore seems unlikely. The operational parameters of this enzyme resemble those of the 17-oxosparteine synthase. Co-operation between the two enzymes would explain why cadaverine is almost undetectable in vivo. 

Pecker, L.R, Hillebrandt, S., Rfigenhagen, C., Herminghaus, S., Landsmann, J. and Berlin, J. (1992) Metabolic effects of a bacterial lysine decarboxylase gene expressed in hairy root culture of Nicotiana glauca. Biotech. Lett., 14, 1035-40. 

Alkaloid metabolism in lupine was proved by Wink and Hartmann to be associated with chloroplasts (34). A series of enzymes involved in the biosynthesis of lupine alkaloids were localized in chloroplasts isolated from leaves of Lupinus polyphylls and seedlings of L. albus by differential centrifugation. They proposed a pathway for the biosynthesis of lupanine via conversion of exogenous 17-oxosparteine to lupanine with intact chloroplasts. The biosynthetic pathway of lupinine was also studied by Wink and Hartmann (35). Two enzymes involved in the biosynthesis of alkaloids, namely, lysine decarboxylase and 17-oxosparteine synthetase, were found in the chloroplast stoma. The activities of the two enzymes were as low as one-thousandth that of diaminopimelate decarboxylase, an enzyme involved in the biosynthetic pathway from lysine to diaminopimelate. It was suggested that these differences are not caused by substrate availability (e,g., lysine concentration) as a critical factor in the synthesis of alkaloids. Feedback inhibition would play a major role in the regulation of amino acid biosynthesis but not in the control of alkaloid formation. 

Guilfoyle, D.E. and Hershfield, I.N. 1996. The survival benefit of short-chain organic acids and the inducible arginine and lysine decarboxylase genes for Escherichia coli. Letters in Applied Microbiology.22 393-396. 

Another bacterium that contributes to commensal biofilms is Eikenella corrodens, a gram negative, small rod (Fig. 13.2c). E. corrodens grows in a healthy oral cavity by reducing nitrate in saliva to nitrite (Sects. 1.3.2 and 12.1.3). It is an important contributor to bite wound infections and is also the major known producer of lysine decarboxylase, which converts lysine to cadaverine and carbon dioxide (Fig. 13.4). Lysine is a nutritionally essential amino acid, whereas cadaverine is not. In humans, E. corrodens and lysine... 

Most cultures from Collection IBSO produce lyases L-ornithine, L-arginine, and L-lysine decarboxylases. Neuraminidase (sialidase, or mucopolysaccharide - N-acetylneuraminilhydrolase) is the enzyme of the hydrolase group. As is usual neuraminidase activity is a property of pathogenic organisms. We found for the first time that luminous bacterial cultures of the species V. harveyi possess low neuraminidase activity. It may be probably one of the factors contributing to contamination of marine animals by luminous bacteria. 

L-Lysine Decarboxylase Origin Bacterium cadaveris Fluka... 

A new gene Idc which encodes lysine decarboxylase was found in addition to the formerly known cadA in Escherichia coli and the enzyme purified from the overexpression strain. The lysine decarboxylase encoded by Idc is constitutively produced by E. coli cells though the cadA encodes an inducible one [9]. It is interesting to know of the existence of this new lysine decarboxylase in lysine-producing Corynebacterium and to investigate the effects of the deletion of the gene on the amounts of L-lysine production. 

Enzymes involved are lysine decarboxylase, a cadaverine transaminase or diamine oxidase and additional enzymes. 

The decarboxylation by lysine decarboxylase of L-lysine (13) to give cadaverine (17) occurs with retention of configuration [protonation occurs on the a-face of the iraine (14)]. The oxidation of cadaverine (17) occurs with loss of the 1-pro-S proton, which is the proton originally sited at C-2 in L-lysine (13) c. Section 1.1). It follows that L-[2- H]lysine should... 

If instead of protonation of the imine function in (14), in the lysine decarboxylase reaction, nucleophilic attack by the 6-amino-group of lysine [see (19)] occurs, (16) is obtained directly and independently of cadaverine, and without loss of the C-2 proton of lysine. This modified" decarboxylase would function, it is suggested, for the biosynthesis of alkaloids such Lysine decarboxylase... 

Lysine decarboxylase Bacillus cadaveris, E. coli L-Lysine Retention 249-251... 

The absolute configuration of 21 was established by two methods. First, 21 was converted to 5-phthalimido[5-2H]valerate by the use of chemical and enzymic methods and shown to have the same optical rotatory properties as those of authentic (5/ )-5-phthalimido[5- H]valerate produced from L-glutamate by an established stereochemical route. Second, 21 was converted to [l- H]cadavarine with L-lysine decarboxylase, followed by treatment with diamine oxidase to form pelletierine. Retention of all of the deuterium in the pelletierine demonstrated that the deuterium must be in the pro-(R) position, since the oxidase reaction is known to labilize hydrogen at the pro-(S) position [Eq. (51)] ... 

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