Publications

• [Production of L-citrulline by a recombinant Corynebacterium crenatum SYPA 5-5 whole-cell biocatalyst].

  Liu Q., Xu M., Zhang R., Wang M., Zhang X., Yang T., Rao Z.

  Arginine deiminase (ADI) was first high-efficient expressed in Corynebacterium crenatum SYPA 5-5. The ADI was purified by Ni-NTA affinity chromatography and SDS-PAGE analysis showed the molecular weight (MW) was 46.8 kDa. The optimal temperature and pH of ADI were 37 ℃ and 6.5 respectively. The Mi ... >> More

  Arginine deiminase (ADI) was first high-efficient expressed in Corynebacterium crenatum SYPA 5-5. The ADI was purified by Ni-NTA affinity chromatography and SDS-PAGE analysis showed the molecular weight (MW) was 46.8 kDa. The optimal temperature and pH of ADI were 37 ℃ and 6.5 respectively. The Michaelis constant was 12.18 mmol/L and the maximum velocity was 0.36 μmol/(min·mL). Under optimal conditions, 300 g/L of arginine was transformed and the productivity reach 8 g/(L·h). The recombinant strain was cultivated in a 5-L fermentor and used for whole-cell transformation of 300 g/L arginine, under repeated-batch bioconversion, the cumulative production reached 1 900 g/L. << Less

  Sheng Wu Gong Cheng Xue Bao 33:1889-1894(2017) [PubMed] [EuropePMC]

• Urea synthesis and metabolism of arginine and citrulline.

  RATNER S.

  Adv Enzymol Relat Subj Biochem 15:319-387(1954) [PubMed] [EuropePMC]

• Arginine deiminase from Mycoplasma arthritidis. Properties of the enzyme from log phase cultures.

  Weickmann J.L., Himmel M.E., Squire P.G., Fahrney D.E.

  Hydrodynamic, chemical, and optical properties of arginine deiminase (EC 3.5.3.6) from Mycoplasma arthritidis are reported for the enzyme isolated from log phase cells. The S020,w and D020,w values of the enzyme are 5.48 S and 5.87 X 10(-7) cm3/s, respectively; the molecular weight is 87,300. Dete ... >> More

  Hydrodynamic, chemical, and optical properties of arginine deiminase (EC 3.5.3.6) from Mycoplasma arthritidis are reported for the enzyme isolated from log phase cells. The S020,w and D020,w values of the enzyme are 5.48 S and 5.87 X 10(-7) cm3/s, respectively; the molecular weight is 87,300. Determination of the amino acid composition shows that about 45% of the residues are nonpolar. Another unique feature of the composition is the presence of 36 half-cystine residues. The state of oxidation of the half-cystines appears to be well established as 16 disulfide and 4 sulfhydryl groups. The reaction of 1 sulfhydryl group with 0.3 mM 5,5'-dithiobis(2-nitrobenzoic acid) has a half-life of about 50 min at pH 8. The modified enzyme retains full activity. Two -SH groups are accessible to this reagent in 2 M guanidine hydrochloride, whereas all 4 -SH groups react immediately in 4 M guanidine hydrochloride. Reduction of disulfide bonds with dithiothreitol occurs only to a limited extent in 8 M urea, but is complete in 4 M guanidine hydrochloride. The enzyme loses activity immediately at pH 2.5, but retains full activity upon standing 8 h at pH 9.5 in several buffers. The large number of cystine residues leads to a complex near ultraviolet circular dichroism spectrum with cystine contributions apparently superimposed on contributions from aromatic residues. The far ultraviolet spectrum suggests that the molecule contains about 18% alpha helix. At pH 2.5, beta conformation and disulfide contributions are dominant. Aromatic and alpha bands are reduced considerably at pH 9.5. << Less

  J Biol Chem 253:6010-6015(1978) [PubMed] [EuropePMC]

• Arginine Deiminase Enzyme Evolving as a Potential Antitumor Agent.

  Somani R.R., Chaskar P.K.

  Some melanomas and hepatocellular carcinomas have been shown to be auxotrophic for arginine. Arginine deiminase (ADI), an arginine degrading enzyme isolated from Mycoplasma, can inhibit the growth of these tumors. It is a catabolizing enzyme which catabolizes arginine to Citrulline. Tumor cells do ... >> More

  Some melanomas and hepatocellular carcinomas have been shown to be auxotrophic for arginine. Arginine deiminase (ADI), an arginine degrading enzyme isolated from Mycoplasma, can inhibit the growth of these tumors. It is a catabolizing enzyme which catabolizes arginine to Citrulline. Tumor cells do not express an enzyme called arginosuccinate synthetase (ASS) and hence, these cells become auxotrophic for arginine. It is found that ADI is specific for arginine and did not degrade other amino acid. This review covers various aspects of ADIs like origin, properties and chemical modifications for better antitumor activity. << Less

  Mini Rev Med Chem 18:363-368(2018) [PubMed] [EuropePMC]

• The arginine dihydrolase system of Streptococcus faecalis. II. Properties of arginine desimidase.

  OGINSKY E.L., GEHRIG R.F.

  J Biol Chem 198:799-805(1952) [PubMed] [EuropePMC]

• Behavior of purified arginine desiminase from S. faecalis.

  PETRACK B., SULLIVAN L., RATNER S.

  Arch Biochem Biophys 69:186-197(1957) [PubMed] [EuropePMC]