EC Number   |
General Information |
Reference |
|---|
    4.1.99.12 | evolution |
angiosperms share a small RIBA gene family consisting of three members. The monofunctional, bipartite RIBA3 proteins AtRIBA2, and AtRIBA3, which have lost DHBPS activity, evolved early in tracheophyte evolution, phylogenetic analysis, overview. While AtRIBA2 is lacking GCHII activity, AtRIBA3 does not display DHBPS function |
-, 727640 |
| 4.1.99.12 | malfunction |
bleaching leaf phenotype of RIBA1 deficient plants, overview. The bleaching phenotype of the seedlings is not counterbalanced by the simultaneous AtRIBA2 and AtRIBA3 expression |
-, 727640 |
| 4.1.99.12 | malfunction |
silencing NbRibA compromises hypersensitive response cell death, NO and ROS production, and induced high susceptibility to oomycete Phytophthora infestans and ascomycete Colletotrichum orbiculare. Compromised radical production and hypersensitive response cell death induced by INF1 in NbRibA-silenced leaves is rescued by adding riboflavin, FMN or FAD |
716533 |
| 4.1.99.12 | metabolism |
3,4-dihydroxy-2-butanone-4-phosphate synthase is one of the key enzymes in the biosynthesis of riboflavin |
-, 728745 |
| 4.1.99.12 | metabolism |
the bifunctional GTP cyclohydrolase II/3,4-dihydroxy-2-butanone 4-phosphate synthase (LcRIBA) catalyzes 2 initial reactions in riboflavin biosynthetic pathway |
748711 |
| 4.1.99.12 | metabolism |
the enzyme is involved in biosynthesis of riboflavin, overview. Riboflavin is the precursor for the synthesis of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which are essential cofactors for numerous enzymes (e.g., dehydrogenases, oxidases, reductases) |
-, 727640 |
| 4.1.99.12 | more |
an essential bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II (DHBPS/GCHII) enzyme from Mycobacterium tuberculosis, Mtb-ribA2. The enzyme is composed of two conformationally different molecules of Mtb-ribA2 in the asymmetric unit that form a dimer via their GCHII domains. DHBPS and GCHII functional homodimers form a long helical-like oligomer, but the enzyme exists as a dimer in solution. The DHBPS subunit possesses an active-site loop1, a substrate channelling loop2, and a pH-sensitive loop3, structure comparisons, overview |
-, 726585 |
| 4.1.99.12 | more |
DHBPS enzyme structure comparisons, active site architecture of enzyme vDHBPS |
-, 748186 |
| 4.1.99.12 | more |
in plants bifunctional RIBA enzymes comprise of N-terminal GTP cyclohydrolase II, GCHII, and C-terminal 3,4-dihydroxy-2-butanone-4-phosphate synthase, DHBPS |
-, 727640 |
| 4.1.99.12 | more |
the two key enzymes of the riboflavin biosynthetic pathway, DHBPS and GTP cyclohydrolaseII (GCHII), EC 3.5.4.25,are fused together into the bifunctional enzyme encoded by Sp0176 gene of Streptococcus pneumoniae strain TIGR 4, DHBPS active site architecture, overview |
-, 728745 |
