EC |
2.5.1.74 |
Accepted name: |
1,4-dihydroxy-2-naphthoate polyprenyltransferase |
Reaction: |
an all-trans-polyprenyl diphosphate + 1,4-dihydroxy-2-naphthoate = a demethylmenaquinone + diphosphate + CO2 |
|
For diagram of vitamin K biosynthesis, click here |
Glossary: |
menaquinone = vitamin K2 |
Systematic name: |
all-trans-polyprenyl-diphosphate:1,4-dihydroxy-2-naphthoate polyprenyltransferase |
Comments: |
This enzyme catalyses a step in the synthesis of menaquinone, in which the prenyl chain synthesized by polyprenyl diphosphate synthase is transferred to 1,4-dihydroxy-2-naphthoate (DHNA). The bacterial enzyme is an inner membrane protein [1], with the C-terminus located in the periplasm [3]. It is highly specific for DHNA but not for a specific length of the prenyl chain [2]. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
References: |
1. |
Shineberg, B. and Young, I.G. Biosynthesis of bacterial menaquinones: the membrane-associated 1,4-dihydroxy-2-naphthoate octaprenyltransferase of Escherichia coli. Biochemistry 15 (1976) 2754–2758. [PMID: 949474] |
2. |
Saito, Y. and Ogura, K. Biosynthesis of menaquinones. Enzymatic prenylation of 1,4-dihydroxy-2-naphthoate by Micrococcus luteus membrane fractions. J. Biochem. 89 (1981) 1445–1452. [PMID: 7275947] |
3. |
Suvarna, K., Stevenson, D., Meganathan, R. and Hudspeth, M.E. Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli. J. Bacteriol. 180 (1998) 2782–2787. [PMID: 9573170] |
4. |
Daley, D.O., Rapp, M., Granseth, E., Melen, K., Drew, D. and von Heijne, G. Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 (2005) 1321–1323. [DOI] [PMID: 15919996] |
|
[EC 2.5.1.74 created 2009] |
|
|
|
|