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Titolo:
Purification of serine racemase: Biosynthesis of the neuromodulator D-serine
Autore:
Wolosker, H; Sheth, KN; Takahashi, M; Mothet, JP; Brady, RO; Ferris, CD; Snyder, SH;
Indirizzi:
Johns Hopkins Univ, Sch Med, Dept Neurosci, Baltimore, MD 21205 USA Johns Hopkins Univ Baltimore MD USA 21205 urosci, Baltimore, MD 21205 USA JohnsUSApkins Univ, Sch Med, Dept Pharmacol & Mol Sci, Baltimore, MD 21205Johns Hopkins Univ Baltimore MD USA 21205 & Mol Sci, Baltimore, MD 21205 Johns Hopkins Univ, Sch Med, Dept Psychiat, Baltimore, MD 21205 USA Johns Hopkins Univ Baltimore MD USA 21205 ychiat, Baltimore, MD 21205 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 2, volume: 96, anno: 1999,
pagine: 721 - 725
SICI:
0027-8424(19990119)96:2<721:POSRBO>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT-BRAIN; NMDA-RECEPTORS; GLYCINE; ACID; RODENTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Snyder, SH Johns1205kins Univ, Sch Med, Dept Neurosci, 725 N Wolfe St, Baltimore, MD 2 Johns Hopkins Univ 725 N Wolfe St Baltimore MD USA 21205 , MD 2
Citazione:
H. Wolosker et al., "Purification of serine racemase: Biosynthesis of the neuromodulator D-serine", P NAS US, 96(2), 1999, pp. 721-725

Abstract

High levels of D-serine occur in mammalian brain, where it appears to be an endogenous ligand of the glycine site of N-methyl-D-aspartate receptors, In glial cul tures of rat cerebral cortex, D-serine is enriched in type II astrocytes and is released upon stimulation with agonists of non-N-methyl-D-aspartate glutamate receptors, The high levels of D-serine in discrete areas of rat brain imply the existence of a biosynthetic pathway, We have purified from rat brain a soluble enzyme that catalyzes the direct racemizationof L-serine to D-serine, Purified serine racemase has a molecular mass of 37 kDa and requires pyridoxal 5'-phosphate for its activity. The enzyme is highly selective toward L-serine, failing to racemize any other amino acid tested. Properties such as pH optimum, K-m values, and the requirement for pyridoxal phosphate resemble those of bacterial racemases, suggesting that the biosynthetic pathway for D-amino acids is conserved from bacteria to mammalian brain.

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Documento generato il 27/10/20 alle ore 10:58:44