KEGG   ENZYME: 4.1.99.29
Entry
EC 4.1.99.29                Enzyme                                 
Name
5,8-dihydroxy-2-naphthoate synthase;
mqnD (gene name);
1,4-dihydroxy-6-naphthoate synthase (incorrect)
Class
Lyases;
Carbon-carbon lyases;
Other carbon-carbon lyases
Sysname
cyclic dehypoxanthine futalosine lyase (dihydroxyacetone-forming)
Reaction(IUBMB)
cyclic dehypoxanthine futalosine = 5,8-dihydroxy-2-naphthoate + dihydroxyacetone
Substrate
cyclic dehypoxanthine futalosine [CPD:C17017]
Product
5,8-dihydroxy-2-naphthoate;
dihydroxyacetone [CPD:C00184]
Comment
The enzyme participates in alternative menaquinone biosynthesis pathways known as the futalosine and modified futalosine pathways, which occurs in some bacterial species including several human pathogens such as Helicobacter pylori, Campylobacter jejuni, and Chlamydia.
History
EC 4.1.99.29 created 2024
Reference
1  [PMID:18801996]
  Authors
Hiratsuka T, Furihata K, Ishikawa J, Yamashita H, Itoh N, Seto H, Dairi T
  Title
An alternative menaquinone biosynthetic pathway operating in microorganisms.
  Journal
Science 321:1670-3 (2008)
DOI:10.1126/science.1160446
  Sequence
[sco:SCO4326]
Reference
2  [PMID:19602440]
  Authors
Arai R, Murayama K, Uchikubo-Kamo T, Nishimoto M, Toyama M, Kuramitsu S, Terada T, Shirouzu M, Yokoyama S.
  Title
Crystal structure of MqnD (TTHA1568), a menaquinone biosynthetic enzyme from Thermus thermophilus HB8.
  Journal
J Struct Biol 168:575-81 (2009)
DOI:10.1016/j.jsb.2009.07.007
  Sequence
[ttj:TTHA1568]
Reference
3  [PMID:34143602]
  Authors
Manion-Sommerhalter HR, Fedoseyenko D, Joshi S, Begley TP.
  Title
Menaquinone Biosynthesis: The Mechanism of 5,8-Dihydroxy-2-naphthoate Synthase (MqnD).
  Journal
Biochemistry 60:1947-1951 (2021)
DOI:10.1021/acs.biochem.1c00257
Other DBs
ExplorEnz - The Enzyme Database: 4.1.99.29
IUBMB Enzyme Nomenclature: 4.1.99.29
ExPASy - ENZYME nomenclature database: 4.1.99.29
BRENDA, the Enzyme Database: 4.1.99.29

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