Cyclic-guanylate-specific phosphodiesterase

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Cyclic-guanylate-specific phosphodiesterase (EC 3.1.4.52, cyclic bis(3->5')diguanylate phosphodiesterase, c-di-GMP-specific phosphodiesterase, c-di-GMP phosphodiesterase, phosphodiesterase, phosphodiesterase A1, PDEA1, VieA) is an enzyme with systematic name cyclic bis(3->5')diguanylate 3-guanylylhydrolase.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

cyclic di-3',5'-guanylate + H₂O

\rightleftharpoons

5'-phosphoguanylyl(3'->5')guanosine

This enzyme requires Mg²⁺ or Mn²⁺ for activity. It is inhibited by Ca²⁺ and Zn²⁺.

References

↑ Chang, A.L., Tuckerman, J.R., Gonzalez, G., Mayer, R., Weinhouse, H., Volman, G., Amikam, D., Benziman, M. and Gilles-Gonzalez, M.A. (2001). "Phosphodiesterase A1, a regulator of cellulose synthesis in Acetobacter xylinum, is a heme-based sensor". Biochemistry 40 (12): 3420–3426. doi:10.1021/bi0100236. PMID 11297407.
↑ Christen, M., Christen, B., Folcher, M., Schauerte, A. and Jenal, U. (2005). "Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP". J. Biol. Chem. 280 (35): 30829–30837. doi:10.1074/jbc.M504429200. PMID 15994307.
↑ Schmidt, A.J., Ryjenkov, D.A. and Gomelsky, M. (2005). "The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains". J. Bacteriol. 187 (14): 4774–4781. doi:10.1128/JB.187.14.4774-4781.2005. PMC 1169503. PMID 15995192.
↑ Tamayo, R., Tischler, A.D. and Camilli, A. (2005). "The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase". J. Biol. Chem. 280 (39): 33324–33330. doi:10.1074/jbc.M506500200. PMC 2776828. PMID 16081414.
↑ Chua SL, Liu Y, Yam JKH, Tolker-Nielsen T, Kjelleberg S, Givskov M, Yang L (2014). "Dispersed cells represent a distinct stage in the transition from bacterial biofilm to planktonic lifestyles". Nature Communications 5. doi:10.1038/ncomms5462.

External links

Cyclic-guanylate-specific phosphodiesterase at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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