• 검색어에 아래의 연산자를 사용하시면 더 정확한 검색결과를 얻을 수 있습니다.
  • 검색연산자
검색연산자 기능 검색시 예
() 우선순위가 가장 높은 연산자 예1) (나노 (기계 | machine))
공백 두 개의 검색어(식)을 모두 포함하고 있는 문서 검색 예1) (나노 기계)
예2) 나노 장영실
| 두 개의 검색어(식) 중 하나 이상 포함하고 있는 문서 검색 예1) (줄기세포 | 면역)
예2) 줄기세포 | 장영실
! NOT 이후에 있는 검색어가 포함된 문서는 제외 예1) (황금 !백금)
예2) !image
* 검색어의 *란에 0개 이상의 임의의 문자가 포함된 문서 검색 예) semi*
"" 따옴표 내의 구문과 완전히 일치하는 문서만 검색 예) "Transform and Quantization"
쳇봇 이모티콘
ScienceON 챗봇입니다.
궁금한 것은 저에게 물어봐주세요.

논문 상세정보

Inhibition of Purine Nucleoside Phosphorylase (PNP) in Micrococcus luteus by Phenylglyoxal

The journal of microbiology v.34 no.3 , 1996년, pp.270 - 273  

Micrococcus luteus purine nucleoside phosphorylase (PNP) has been purified and characterized. The physical and kinetic properties have been described previously. Chemical modification of the enzyme was attempted to gain insight on the active site. The enzyme was inactivated in a time-dependent manner by the arginine- specific modifying reagent phenylglyoxal. There was a linear relationship between the observed rate of inactivation and the phenylglyoxal concentration. At 30 $^{\circ}C$ the bimolecular rate constant for the modification was 0.015 $min^{-1}mM^{-1}$ in 50 mM $NaHCO_3$ buffer, pH 7.5. The plot of logk versus log phenylglyoxal concentration was a strainght line with a slope value of 0.9, indicating that modification of one arginine residue was needed to inactivate the enzyme. Preincubation with saturated solutions of substrates protected the enzyme from inhibition of phenylglyoxal, indicating that reactions with phenylglyoxal were directed at arginyl residues essential for the catalytic functioning of the enzyme.

참고문헌 (12)

  1. Purification and Characterization of PNP in Micrococcus luteus , Choi, H.S. , Kor. J. Microbiol. / v.34,pp.82-89, 1996
  2. Purification and characterization of a novel nucleoside phosphorylase from a Krebsiella sp. and its use in the enzymatic production of adenosine arabinoside , Ling, F.;Inou, Y.;Kimura, A. , Appl. Environment. Microbiol. / v.56,pp.3830-3834, 1990
  3. Inactivation of myosin by 2,4-dinitrophenol and protection by adenosine triphosphate and other phosphate compounds , Levy, H.M.;Leber P.D.;Ryan, E.M. , J. Biol. Chem. / v.238,pp.3654-3659, 1963
  4. Kinetics of inactivation of Escherichia coli glutamate apodecarboxylase by phenyl glyoxal , Cheung, S.;Fonda, M.L. , Arch. Biochem. Biophys / v.198,pp.541-547, 1979
  5. Arginine 304 is an active site residue in phosphomannose isomerase from Candida albicans , Wells, T.N.C.;Scully, P.;Magnenat, E. , Biochemistry / v.33,pp.5777-5782, 1994
  6. Functionally important arginine residues of aspartate transcarbamylase , Kantrowitz, E.R.;Lipscomb, W.N. , J. Biol. Chem. / v.251,pp.2688-2695, 1976
  7. Purine nucleoside phosphorylase from Eschrichia coli and Salmonella typhymurium , Jensen, K.F.;Nygaard, P. , Eur. J. Biochem. / v.51,pp.253-265, 1975
  8. Essential arginyl residues in Escherichia coli alkaline phosphatase , Daemen, F.J.M.;riordan, J.F. , Biochemistry / v.13,pp.2865-2871, 1974
  9. An essential arginine residue in porcine phospholipase A2 , Vensel, L. A.;Kantrowitz, E.R. , J. Biol. Chem. / v.255,pp.7306-7310, 1980
  10. Kinetic analysis of purine nucleoside phosphorylase in Saccharomyces cerevisiae , Choi, H.S. , Kor. J. Microbiol. / v.31,pp.148-156, 1993
  11. Purine nucleoside phosphorylase , Stoeckler, J.D. , Developments in Cancer Chemotherapy / v.,pp.35-60, 1984
  12. Reaction of phenylglyoxal with arginine groups in D-amino acid oxidase from Rhodotrorula gracilis , Gadda, G.;Negri, A.;Pilone, M.S. , J. Biol. Chem. / v.269,pp.17809-17814, 1994

이 논문을 인용한 문헌 (0)

  1. 이 논문을 인용한 문헌 없음


원문 PDF 다운로드

  • ScienceON :

원문 URL 링크

원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다. (원문복사서비스 안내 바로 가기)

상세조회 0건 원문조회 0건

DOI 인용 스타일