Propionate kinase

Identifiers
EC no.| 2.7.2.15
CAS no.| 39369-28-3
Databases
IntEnz| IntEnz view
BRENDA| BRENDA entry
ExPASy| NiceZyme view
KEGG| KEGG entry
MetaCyc| metabolic pathway
PRIAM| profile
PDB structures| RCSB PDB PDBe PDBsum
| Search

PMC| articles
PubMed| articles
NCBI| proteins

Propionate kinase (EC 2.7.2.15, PduW, TdcD, propionate/acetate kinase) is an enzyme with systematic name ATP:propanoate phosphotransferase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

ATP + propanoate ⇌ {\displaystyle \rightleftharpoons } ADP + propanoyl phosphate

This enzyme requires Mg2+.

## References

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1. ^ Hesslinger C, Fairhurst SA, Sawers G (January 1998). "Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate". Molecular Microbiology. 27 (2): 477–92\. doi:10.1046/j.1365-2958.1998.00696.x. PMID 9484901.
2. ^ Palacios S, Starai VJ, Escalante-Semerena JC (May 2003). "Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and propionate catabolic pathways needed for expression of the prpBCDE operon during growth of Salmonella enterica on 1,2-propanediol". Journal of Bacteriology. 185 (9): 2802–10\. doi:10.1128/jb.185.9.2802-2810.2003. PMC 154405. PMID 12700259.
3. ^ Wei Y, Miller CG (October 1999). "Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium". Journal of Bacteriology. 181 (19): 6092–7\. PMC 103637. PMID 10498722.
4. ^ Ingram-Smith C, Gorrell A, Lawrence SH, Iyer P, Smith K, Ferry JG (April 2005). "Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase". Journal of Bacteriology. 187 (7): 2386–94\. doi:10.1128/jb.187.7.2386-2394.2005. PMC 1065240. PMID 15774882.
5. ^ Simanshu DK, Murthy MR (January 2005). "Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium". Acta Crystallographica Section F. 61 (Pt 1): 52–5\. doi:10.1107/s1744309104026429. PMC 1952409. PMID 16508089.
6. ^ Simanshu DK, Savithri HS, Murthy MR (September 2005). "Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily". Journal of Molecular Biology. 352 (4): 876–92\. doi:10.1016/j.jmb.2005.07.069. PMID 16139298.

## External links

[edit]

* Propionate+kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

* v
* t
* e

Transferases: phosphorus-containing groups (EC 2.7)

2.7.1-2.7.4:
phosphotransferase/kinase
(PO4)|

| 2.7.1: OH acceptor|

* Hexo-
* Gluco-
* Fructo-
* Hepatic
* Galacto-
* Phosphofructo-
* 1
* Liver
* Muscle
* Platelet
* 2
* Riboflavin
* Shikimate
* Thymidine
* ADP-thymidine
* NAD+
* Glycerol
* Pantothenate
* Mevalonate
* Pyruvate
* Deoxycytidine
* PFP
* Diacylglycerol
* Phosphoinositide 3
* Class I PI 3
* Class II PI 3
* Sphingosine
* Glucose-1,6-bisphosphate synthase

|

2.7.2: COOH acceptor|

* Phosphoglycerate
* Aspartate kinase

2.7.3: N acceptor|

* Creatine

2.7.4: PO4 acceptor|

* Phosphomevalonate
* Adenylate
* Nucleoside-diphosphate
* Uridylate
* Guanylate
* Thiamine-diphosphate

2.7.6: diphosphotransferase
(P2O7)|

* Ribose-phosphate diphosphokinase
* Thiamine diphosphokinase

2.7.7: nucleotidyltransferase
(PO4-nucleoside)|

| Polymerase|

| DNA polymerase|

DNA-directed DNA polymerase
I/A

Taq
II/B

Pfu
III/C
IV/X

TDT
V/Y

RNA-directed DNA polymerase
Reverse transcriptase

Telomerase

|

RNA polymerase|

Template-directed
RNA polymerase I

III

ssRNAP

POLRMT
Primase

PrimPol
RNA-dependent RNA polymerase
Polyadenylation
PAP
PNPase

Phosphorolytic
3' to 5' exoribonuclease|

* RNase PH
* PNPase

Nucleotidyltransferase|

* UTP—glucose-1-phosphate uridylyltransferase
* Galactose-1-phosphate uridylyltransferase

Guanylyltransferase|

* mRNA capping enzyme

Other|

* Recombinase (Integrase)
* Transposase

2.7.8: miscellaneous|

| Phosphatidyltransferases|

* CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase
* CDP-diacylglycerol—serine O-phosphatidyltransferase
* CDP-diacylglycerol—inositol 3-phosphatidyltransferase
* CDP-diacylglycerol—choline O-phosphatidyltransferase

|

Glycosyl-1-phosphotransferase|

* N-acetylglucosamine-1-phosphate transferase

2.7.10-2.7.13: protein kinase
(PO4; protein acceptor)|

| 2.7.10: protein-tyrosine|

* see tyrosine kinases

|

2.7.11: protein-serine/threonine|

* see serine/threonine-specific protein kinases

2.7.12: protein-dual-specificity|

* see serine/threonine-specific protein kinases

2.7.13: protein-histidine|

* Protein-histidine pros-kinase
* Protein-histidine tele-kinase
* Histidine kinase

* v
* t
* e

Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)
* EC7 Translocases (list)

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* Biology

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