TY  - JOUR
AU  - Marienhagen, J.
AU  - Kennerknecht, N.
AU  - Sahm, H.
AU  - Eggeling, L.
TI  - Functional analysis of all aminotransferase proteins inferred from the genome sequence of Corynebacterium glutamicum
JO  - Journal of bacteriology
VL  - 187
SN  - 0021-9193
CY  - Washington, DC
PB  - Soc.
M1  - PreJuSER-47527
SP  - 7639 - 7646
PY  - 2005
N1  - Record converted from VDB: 12.11.2012
AB  - Twenty putative aminotransferase (AT) proteins of Corynebacterium glutamicum, or rather pyridoxal-5'-phosphate (PLP)-dependent enzymes, were isolated and assayed among others with L-glutamate, L-aspartate, and L-alanine as amino donors and a number of 2-oxo-acids as amino acceptors. One outstanding AT identified is AlaT, which has a broad amino donor specificity utilizing (in the order of preference) L-glutamate > 2-aminobutyrate > L-aspartate with pyruvate as acceptor. Another AT is AvtA, which utilizes L-alanine to aminate 2-oxo-isovalerate, the L-valine precursor, and 2-oxo-butyrate. A second AT active with the L-valine precursor and that of the other two branched-chain amino acids, too, is IlvE, and both enzyme activities overlap partially in vivo, as demonstrated by the analysis of deletion mutants. Also identified was AroT, the aromatic AT, and this and IlvE were shown to have comparable activities with phenylpyruvate, thus demonstrating the relevance of both ATs for L-phenylalanine synthesis. We also assessed the activity of two PLP-containing cysteine desulfurases, supplying a persulfide intermediate. One of them is SufS, which assists in the sulfur transfer pathway for the Fe-S cluster assembly. Together with the identification of further ATs and the additional analysis of deletion mutants, this results in an overview of the ATs within an organism that may not have been achieved thus far.
KW  - Alanine: metabolism
KW  - Aspartic Acid: metabolism
KW  - Bacterial Proteins: genetics
KW  - Bacterial Proteins: isolation & purification
KW  - Bacterial Proteins: metabolism
KW  - Butyric Acids: metabolism
KW  - Carbon-Sulfur Lyases: metabolism
KW  - Corynebacterium glutamicum: enzymology
KW  - Corynebacterium glutamicum: genetics
KW  - Gene Deletion
KW  - Glutamic Acid: metabolism
KW  - Keto Acids: metabolism
KW  - Phenylpyruvic Acids: metabolism
KW  - Pyruvic Acid: metabolism
KW  - Substrate Specificity
KW  - Transaminases: genetics
KW  - Transaminases: isolation & purification
KW  - Transaminases: metabolism
KW  - Bacterial Proteins (NLM Chemicals)
KW  - Butyric Acids (NLM Chemicals)
KW  - Keto Acids (NLM Chemicals)
KW  - Phenylpyruvic Acids (NLM Chemicals)
KW  - Pyruvic Acid (NLM Chemicals)
KW  - alpha-keto-beta-methylvaleric acid (NLM Chemicals)
KW  - phenylpyruvic acid (NLM Chemicals)
KW  - Alanine (NLM Chemicals)
KW  - Aspartic Acid (NLM Chemicals)
KW  - Glutamic Acid (NLM Chemicals)
KW  - alpha-ketobutyric acid (NLM Chemicals)
KW  - alpha-ketoisovalerate (NLM Chemicals)
KW  - alpha-ketoisocaproic acid (NLM Chemicals)
KW  - Transaminases (NLM Chemicals)
KW  - Carbon-Sulfur Lyases (NLM Chemicals)
KW  - cysteine desulfurase (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:16267288
C2  - pmc:PMC1280304
UR  - <Go to ISI:>//WOS:000233400200011
DO  - DOI:10.1128/JB.187.22.7639-7646.2005
UR  - https://juser.fz-juelich.de/record/47527
ER  -