Propionate kinase

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PubMed	các bài viết
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Propionate kinase
Mã định danh (ID)
Mã EC	2.7.2.15
Mã CAS	39369-28-3
Các dữ liệu thông tin
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	chu trình chuyển hóa
PRIAM	profile
Các cấu trúc PDB	RCSB PDB PDBj PDBe PDBsum
Nghiên cứu
PMC	các bài viết
PubMed	các bài viết
NCBI	các protein

Propionate kinase (EC 2.7.2.15, PduW, TdcD, Propionate / acetate kinase) là một enzym có tên hệ thống ATP: phosphotransferase propanoate.^[1]^[2]^[3]^[4]^[5]^[6] Enzyme này xúc tác phản ứng hóa học sau:

ATP + propanoate

\rightleftharpoons

ADP + propanoyl phosphate

Enzym này đòi hỏi Mg²⁺.

Tham khảo[sửa | sửa mã nguồn]

^ Heßlinger, C.; Fairhurst, S.A.; Sawers, G. (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”. Mol. Microbiol. 27: 477–492. doi:10.1046/j.1365-2958.1998.00696.x. PMID 9484901.
^ Palacios, S.; Starai, V.J.; Escalante-Semerena, J.C. (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”. J. Bacteriol. 185: 2802–2810. doi:10.1128/jb.185.9.2802-2810.2003. PMC 154405. PMID 12700259.
^ Wei, Y.; Miller, C.G. (1999). “Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium”. J. Bacteriol. 181: 6092–6097. PMC 103637. PMID 10498722.
^ Ingram-Smith, C.; Gorrell, A.; Lawrence, S.H.; Iyer, P.; Smith, K.; Ferry, J.G. (2005). “Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase”. J. Bacteriol. 187: 2386–2394. doi:10.1128/jb.187.7.2386-2394.2005. PMC 1065240. PMID 15774882.
^ Simanshu, D.K. (2005). “Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium”. Acta Crystallogr. F. 61: 52–55. doi:10.1107/s1744309104026429. PMC 1952409. PMID 16508089.
^ Simanshu, D.K.; Savithri, H.S.; Murthy, M.R. (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”. J. Mol. Biol. 352: 876–892. doi:10.1016/j.jmb.2005.07.069. PMID 16139298.

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[1] Heßlinger, C.; Fairhurst, S.A.; Sawers, G. (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”. Mol. Microbiol. 27: 477–492. doi:10.1046/j.1365-2958.1998.00696.x. PMID 9484901.

[2] Palacios, S.; Starai, V.J.; Escalante-Semerena, J.C. (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”. J. Bacteriol. 185: 2802–2810. doi:10.1128/jb.185.9.2802-2810.2003. PMC 154405. PMID 12700259.

[3] Wei, Y.; Miller, C.G. (1999). “Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium”. J. Bacteriol. 181: 6092–6097. PMC 103637. PMID 10498722.

[4] Ingram-Smith, C.; Gorrell, A.; Lawrence, S.H.; Iyer, P.; Smith, K.; Ferry, J.G. (2005). “Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase”. J. Bacteriol. 187: 2386–2394. doi:10.1128/jb.187.7.2386-2394.2005. PMC 1065240. PMID 15774882.

[5] Simanshu, D.K. (2005). “Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium”. Acta Crystallogr. F. 61: 52–55. doi:10.1107/s1744309104026429. PMC 1952409. PMID 16508089.

[6] Simanshu, D.K.; Savithri, H.S.; Murthy, M.R. (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”. J. Mol. Biol. 352: 876–892. doi:10.1016/j.jmb.2005.07.069. PMID 16139298.

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