Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

Reference on EC 4.1.2.50 - 6-carboxytetrahydropterin synthase

Please use the Reference Search for a specific query.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McCarty, R.M.; Somogyi, A.; Bandarian, V.
Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase
Biochemistry
48
2301-2303
2009
Escherichia coli
Manually annotated by BRENDA team
Cicmil, N.; Shi, L.
Crystallization and preliminary X-ray characterization of queD from Bacillus subtilis, an enzyme involved in queuosine biosynthesis
Acta Crystallogr. Sect. F
64
119-122
2008
Bacillus subtilis
Manually annotated by BRENDA team
Seo, K.H.; Zhuang, N.; Park, Y.S.; Park, K.H.; Lee, K.H.
Structural basis of a novel activity of bacterial 6-pyruvoyltetrahydropterin synthase homologues distinct from mammalian 6-pyruvoyltetrahydropterin synthase activity
Acta Crystallogr. Sect. D
70
1212-1223
2014
Escherichia coli (P65870), Escherichia coli
Manually annotated by BRENDA team
Miles, Z.D.; Roberts, S.A.; McCarty, R.M.; Bandarian, V.
Biochemical and structural studies of 6-carboxy-5,6,7,8-tetrahydropterin synthase reveal the molecular basis of catalytic promiscuity within the tunnel-fold superfamily
J. Biol. Chem.
289
23641-23652
2014
Escherichia coli (P65870)
Manually annotated by BRENDA team