Regulatory Properties of the ADP-Glucose Pyrophosphorylase from the Clostridial Firmicutes Member Ruminococcus albus

Antonela E. Cereijo; Matías D. Asencion Diez; Miguel A. Ballicora; Alberto A. Iglesias

doi:10.1128/jb.00172-18

Regulatory Properties of the ADP-Glucose Pyrophosphorylase from the Clostridial Firmicutes Member Ruminococcus albus

Antonela E. Cereijo, Matías D. Asencion Diez, Miguel A. Ballicora, Alberto A. Iglesias

Department of Chemistry and Biochemistry

Spanish National Research Council

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

Original language	American English
Journal	Journal of Bacteriology
Volume	200
Issue number	17
DOIs	https://doi.org/10.1128/jb.00172-18
State	Published - Jun 25 2018

Disciplines

Biochemistry
Biology

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@article{b784227d689547f0ad88f91e86d2c1bd,

title = "Regulatory Properties of the ADP-Glucose Pyrophosphorylase from the Clostridial Firmicutes Member Ruminococcus albus",

author = "Cereijo, \{Antonela E.\} and Diez, \{Mat{\'i}as D. Asencion\} and Ballicora, \{Miguel A.\} and Iglesias, \{Alberto A.\}",

note = "ADP-glucose pyrophosphorylase from Firmicutes is encoded by two genes ( glgC and glgD ) leading to a heterotetrameric protein structure, unlike those in other bacterial phyla. The enzymes from two groups of Firmicutes, Bacillales and Lactobacillales, present dissimilar kinetic and regulatory properties. Nevertheless, no ADP-glucose pyrophosphorylase from Clostridiales, the third group in Firmicutes, has been characterized.",

year = "2018",

month = jun,

day = "25",

doi = "10.1128/jb.00172-18",

language = "American English",

volume = "200",

journal = "Journal of Bacteriology",

issn = "1098-5530",

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T1 - Regulatory Properties of the ADP-Glucose Pyrophosphorylase from the Clostridial Firmicutes Member Ruminococcus albus

AU - Cereijo, Antonela E.

AU - Diez, Matías D. Asencion

AU - Ballicora, Miguel A.

AU - Iglesias, Alberto A.

N1 - ADP-glucose pyrophosphorylase from Firmicutes is encoded by two genes ( glgC and glgD ) leading to a heterotetrameric protein structure, unlike those in other bacterial phyla. The enzymes from two groups of Firmicutes, Bacillales and Lactobacillales, present dissimilar kinetic and regulatory properties. Nevertheless, no ADP-glucose pyrophosphorylase from Clostridiales, the third group in Firmicutes, has been characterized.

PY - 2018/6/25

Y1 - 2018/6/25

UR - https://jb.asm.org/content/200/17/e00172-18

U2 - 10.1128/jb.00172-18

DO - 10.1128/jb.00172-18

M3 - Article

SN - 1098-5530

VL - 200

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 17

ER -

Regulatory Properties of the ADP-Glucose Pyrophosphorylase from the Clostridial Firmicutes Member Ruminococcus albus

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