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Titolo:
IRON-SULFUR CLUSTER-CONTAINING L-SERINE DEHYDRATASE FROM PEPTOSTREPTOCOCCUS-ASACCHAROLYTICUS - CORRELATION OF THE CLUSTER TYPE WITH ENZYMATIC-ACTIVITY
Autore:
HOFMEISTER AEM; ALBRACHT SPJ; BUCKEL W;
Indirizzi:
UNIV MARBURG,FACHBEREICH BIOL,MIKROBIOL LAB,KARL FRISCH STR D-35032 MARBURG GERMANY UNIV MARBURG,FACHBEREICH BIOL,MIKROBIOL LAB D-35032 MARBURG GERMANY UNIV AMSTERDAM,EC SLATER INST BIOCHEM RES,BIOCENTRUM AMSTERDAM 1018 TV AMSTERDAM NETHERLANDS
Titolo Testata:
FEBS letters
fascicolo: 3, volume: 351, anno: 1994,
pagine: 416 - 418
SICI:
0014-5793(1994)351:3<416:ICLDFP>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROSTHETIC GROUPS; L-THREONINE; ENZYMES; PROTEINS;
Keywords:
L-SERINE DEHYDRATASE; ELECTRON PARAMAGNETIC RESONANCE; [3FE-4S](+) CLUSTER; [4F-4S](2+) CLUSTER; NONREDOX IRON-SULFUR PROTEIN; PEPTOSTREPTOCOCCUS ASACCHAROLYTICUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
11
Recensione:
Indirizzi per estratti:
Citazione:
A.E.M. Hofmeister et al., "IRON-SULFUR CLUSTER-CONTAINING L-SERINE DEHYDRATASE FROM PEPTOSTREPTOCOCCUS-ASACCHAROLYTICUS - CORRELATION OF THE CLUSTER TYPE WITH ENZYMATIC-ACTIVITY", FEBS letters, 351(3), 1994, pp. 416-418

Abstract

Investigations were performed with regard to the function of the iron-sulfur cluster of L-serine dehydratase from Peptostreptococcus asaccharolyticus, an enzyme which is novel in the class of deaminating hydro-lyases in that it lacks pyridoxal-5'-phosphate. Anaerobically purified L-serine dehydratase from P. asaccharolyticus revealed EPR spectra characteristic of a [3Fe-4S](+) cluster constituting 1% of the total enzyme concentration. Upon incubation of the enzyme under air the intensity of the [3Fe-4S](+) signal increased correlating with the loss of enzymatic activity. Addition of L-serine prevented this. Hence, active L-serine dehydratase probably contains a diamagnetic [4Fe-4S](2+) cluster which is converted by oxidation and loss of one iron ion to a paramagnetic [3Fe-4S](+) cluster, resulting in inactivation of the enzyme. In analogy to the mechanism elucidated for aconitase, it is proposed that L-serine is coordinated via its hydroxyl and carboxyl groups to the labile iron atom of the [4Fe4S](2+) cluster.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 06:27:45