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Titolo:
Purification and characterization of alanine racemase from hepatopancreas of black-tiger prawn, Penaeus monodon
Autore:
Uo, T; Ueda, M; Nishiyama, T; Yoshimura, T; Esaki, N;
Indirizzi:
Kyoto Univ, Inst Chem Res, Kyoto 6110011, Japan Kyoto Univ Kyoto Japan 6110011 Univ, Inst Chem Res, Kyoto 6110011, Japan
Titolo Testata:
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
fascicolo: 1-6, volume: 12, anno: 2001,
pagine: 137 - 144
SICI:
1381-1177(20010228)12:1-6<137:PACOAR>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
D-SERINE; ALPHA-AMYLASE; D-AMINO; ALTEROMONAS-HALOPLANCTIS; SEAWATER ACCLIMATION; D-ASPARTATE; BIOSYNTHESIS; INACTIVATION; CHLORIDE; CRAYFISH;
Keywords:
D-alanine; alanine racemase; prawn; osmoregulation; pyridoxal 5 '-phosphate;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Esaki, N Kyoto Univ, Inst Chem Res, Kyoto 6110011, Japan Kyoto Univ Kyoto Japan 6110011 t Chem Res, Kyoto 6110011, Japan
Citazione:
T. Uo et al., "Purification and characterization of alanine racemase from hepatopancreas of black-tiger prawn, Penaeus monodon", J MOL CAT B, 12(1-6), 2001, pp. 137-144

Abstract

Alanine racemase has been purified to homogeneity from the hepatopancreas of the black tiger prawn. Panaeus mondon. The enzyme depends on pyridoxal 5'-phosphate and consists of two subunits with an identical molecular weightof 41,000. V-max and K-m values for L-alanine are 460 mu mol/min/mg and 50mM, and those for D-alanine are 94 mu mol/min/mg and 24 mM, respectively. The enzyme is highly specific toward alanine. Among other amino acids examined, only serine served as a substrate: L-serine was racemized at a rate ofapproximately 0.5% of that of L-alanine. The prawn enzyme is immunochemically distinguishable from the enzymes of Bacillus stearothermophilus and Schizosaccharomyces pombe, which resemble each other. The prawn enzyme is activated and stabilized by the presence of monovalent anions including chloride. This is consistent with the previous hypothesis (e.g. E. Fujita, E. Okuma, H. Abe, Comp. Biochem. Physiol. 116A (1997) 83-87) that D-alanine servesas an osmoregulator in marine and euryhaline animals. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 00:10:54