Site-directed mutagenesis of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Binding of the peripheral components E1p and E3.

E. Schulze; A.H. Westphal; H. Boumans; A. de Kok

Site-directed mutagenesis of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Binding of the peripheral components E1p and E3.

E. Schulze, A.H. Westphal, H. Boumans, A. de Kok

Biochemistry

Research output: Contribution to journal › Article › Academic › peer-review

Original language	English
Pages (from-to)	841-848
Journal	European Journal of Biochemistry
Volume	202
Publication status	Published - 1991

Cite this

@article{3b395d56fdf64597b06b66fc3849328a,

title = "Site-directed mutagenesis of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Binding of the peripheral components E1p and E3.",

author = "E. Schulze and A.H. Westphal and H. Boumans and {de Kok}, A.",

year = "1991",

language = "English",

volume = "202",

pages = "841--848",

journal = "European Journal of Biochemistry",

issn = "0014-2956",

publisher = "Wiley-Blackwell Publishing Ltd",

}

Site-directed mutagenesis of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Binding of the peripheral components E1p and E3. / Schulze, E.; Westphal, A.H.; Boumans, H. et al.
In: European Journal of Biochemistry, Vol. 202, 1991, p. 841-848.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - Site-directed mutagenesis of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Binding of the peripheral components E1p and E3.

AU - Schulze, E.

AU - Westphal, A.H.

AU - Boumans, H.

AU - de Kok, A.

PY - 1991

Y1 - 1991

M3 - Article

SN - 0014-2956

VL - 202

SP - 841

EP - 848

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

ER -