The C-terminal domain of Escherichia coli dihydrodipicolinate synthase (DHDPS) is essential for maintenance of quaternary structure and efficient catalysis

Belinda Guo; S R A Devenish; R C J Dobson; A C Muscroft-Taylor; J A Gerrard

doi:10.1016/j.bbrc.2009.01.169

The C-terminal domain of Escherichia coli dihydrodipicolinate synthase (DHDPS) is essential for maintenance of quaternary structure and efficient catalysis

Belinda Guo, S R A Devenish, R C J Dobson, A C Muscroft-Taylor, J A Gerrard

Research output: Contribution to journal › Article

Original language	English
Pages (from-to)	802-806
Journal	Biochemical and Biophysical Research Communications
Volume	380
DOIs	https://doi.org/10.1016/j.bbrc.2009.01.169
Publication status	Published - 2012

Access to Document

10.1016/j.bbrc.2009.01.169

Cite this

@article{95c79e6ee2104c73a3018e247ea20b14,

title = "The C-terminal domain of Escherichia coli dihydrodipicolinate synthase (DHDPS) is essential for maintenance of quaternary structure and efficient catalysis",

author = "Belinda Guo and Devenish, {S R A} and Dobson, {R C J} and Muscroft-Taylor, {A C} and Gerrard, {J A}",

year = "2012",

doi = "10.1016/j.bbrc.2009.01.169",

language = "English",

volume = "380",

pages = "802--806",

journal = "Biochemistry Biophysics Research Communications",

issn = "0006-291X",

publisher = "Academic Press",

}

The C-terminal domain of Escherichia coli dihydrodipicolinate synthase (DHDPS) is essential for maintenance of quaternary structure and efficient catalysis. / Guo, Belinda; Devenish, S R A; Dobson, R C J; Muscroft-Taylor, A C; Gerrard, J A.

In: Biochemical and Biophysical Research Communications, Vol. 380, 2012, p. 802-806.

Research output: Contribution to journal › Article

TY - JOUR

T1 - The C-terminal domain of Escherichia coli dihydrodipicolinate synthase (DHDPS) is essential for maintenance of quaternary structure and efficient catalysis

AU - Guo, Belinda

AU - Devenish, S R A

AU - Dobson, R C J

AU - Muscroft-Taylor, A C

AU - Gerrard, J A

PY - 2012

Y1 - 2012

U2 - 10.1016/j.bbrc.2009.01.169

DO - 10.1016/j.bbrc.2009.01.169

M3 - Article

C2 - 19338756

VL - 380

SP - 802

EP - 806

JO - Biochemistry Biophysics Research Communications

JF - Biochemistry Biophysics Research Communications

SN - 0006-291X

ER -