Methanogens with pseudomurein use diaminopimelate aminotransferase in lysine biosynthesis.
FEBS Lett
; 582(9): 1369-74, 2008 Apr 16.
Article
em En
| MEDLINE
| ID: mdl-18371309
ABSTRACT
Methanothermobacter thermautotrophicus uses lysine for both protein synthesis and cross-linking pseudomurein in its cell wall. A diaminopimelate aminotransferase enzyme from this methanogen (MTH0052) converts tetrahydrodipicolinate to l,l-diaminopimelate, a lysine precursor. This gene complemented an Escherichia coli diaminopimelate auxotrophy, and the purified protein catalyzed the transamination of diaminopimelate to tetrahydrodipicolinate. Phylogenetic analysis indicated this gene was recruited from anaerobic Gram-positive bacteria. These results expand the family of diaminopimelate aminotransferases to a diverse set of plant, bacterial and archaeal homologs. In contrast marine methanogens from the Methanococcales, which lack pseudomurein, appear to use a different diaminopimelate pathway for lysine biosynthesis.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptidoglicano
/
Methanobacteriaceae
/
Transaminases
/
Lisina
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2008
Tipo de documento:
Article
País de afiliação:
Estados Unidos