Information on EC 4.1.99.12 -

Information on EC 4.1.99.12 - 3,4-dihydroxy-2-butanone-4-phosphate synthase:

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EC NUMBER	COMMENTARY
4.1.99.12	-

RECOMMENDED NAME	GeneOntology No.
3,4-dihydroxy-2-butanone-4-phosphate synthase	GO:0008686

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate		-	-	-	-
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate		active site architecture	Methanocaldococcus jannaschii	-	671038
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate		active site structure and catalytic mechanism, modeling of the substrate ribulose 5-phosphate bound in the active site with the phosphate group anchored at the sulfate site and the placement of the ribulose group guided by the glycerol site, the catalytic reaction involves residues Asp41, Cys66, and Glu174, and the Asp99-His136 dyad	Magnaporthe grisea	-	671958
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate		catalytic mechanism	Escherichia coli	-	673430
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate		catalytic mechanism	Meyerozyma guilliermondii	-	674403
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate		reaction mechanism involving intramolecular skeletal rearrangement, a cluster of charged amino acid residues comprising Arg25, Glu26 and Glu28, Asp21 and Asp30 is essential for catalytic activity, as well as His164 and Glu185	Methanocaldococcus jannaschii	-	674406
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate		active site and reaction mechanism, structure-function relationship, structural coordination spheres are important, residues of the first coordination sphere involved in metal binding are indispensable for catalytic activity, Glu185 is essential for catalytic activity	Methanocaldococcus jannaschii	Q60364	674408
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate		RibA is a bifunctional enzyme possessing 3,4-dihydroxy-2-butanone 4-phosphate synthase activity located in the N-terminal half of the protein and GTP cyclohydrolase II activity, EC 3.5.4.25, of the C-terminal domain, overview	Bacillus subtilis	-	675226
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate		reaction mechanism, the enzyme possesses an essential acidic active-site loop	Candida albicans	Q5A3V6	675342
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate		reaction mechanism	Escherichia coli	-	675576
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate		catalytic mechanism	Escherichia coli K-12	P0A7J0	675800
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate		catalytic reaction mechanism, substrate recognition and active site structure, active site consists of three glutamates, two aspartates, two histidines, and a cysteine which may provide the means for general acid and base catalysis and for coordinating the Mg2+ cofactor within the active site	Escherichia coli	-	677168

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

PATHWAY	KEGG Link	MetaCyc Link
flavin biosynthesis I (bacteria and plants)	-	RIBOSYN2-PWY
flavin biosynthesis II (archaea)	-	PWY-6167
flavin biosynthesis III (fungi)	-	PWY-6168

SYSTEMATIC NAME

IUBMB Comments

D-ribulose 5-phosphate formate-lyase (L-3,4-dihydroxybutan-2-one 4-phosphate-forming)

Requires a divalent cation, preferably Mg2+, for activity [1]. The reaction involves an intramolecular skeletal rearrangement, with the bonds in D-ribulose 5-phosphate that connect C-3 and C-5 to C-4 being broken, C-4 being removed as formate and reconnection of C-3 and C-5 [1]. The phosphorylated four-carbon product (L-3,4-dihydroxybutan-2-one 4-phosphate) is an intermediate in the biosynthesis of riboflavin [1].

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
3,4-dihydroxy 2-butanone-4-phosphate synthase	Mycobacterium tuberculosis	A5U2B7	-	716058
3,4-dihydroxy-2-butanone 4-phosphate synthase	Methanocaldococcus jannaschii	-	-	671038, 674408
3,4-dihydroxy-2-butanone 4-phosphate synthase	Escherichia coli	-	-	673430, 675576, 677168, 703578
3,4-dihydroxy-2-butanone 4-phosphate synthase	Candida albicans	-	-	675342, 690233
3,4-dihydroxy-2-butanone-4-phosphate synthase	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	-	716877
DBPS	Methanocaldococcus jannaschii	Q60364	-	674408
DHBP synthase	Saccharomyces cerevisiae	-	-	674407
DHBP synthase	Escherichia coli K-12	P0A7J0	-	675800
DHBP synthase	Escherichia coli	-	-	703578
DHBPS	Methanocaldococcus jannaschii	-	-	671038, 676912
DHBPS	Candida albicans	-	-	675342, 690233
DHBPS	Escherichia coli	-	-	676912
DHBPS	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	-	716877
dihydroxybutanone phosphate synthase	Magnaporthe grisea	-	-	671037
dihydroxybutanone phosphate synthase	Saccharomyces cerevisiae	-	-	674407
L-3,4-dihydroxy-2-butanone 4-phosphate synthase	Meyerozyma guilliermondii	-	-	674403
Mtb-DHBPS	Mycobacterium tuberculosis	A5U2B7	-	716058
NbRibA	Nicotiana benthamiana	-	bifunctional enzyme: guanosine triphosphate cyclohydrolase II/3,4-dihydroxy-2-butanone-4-phosphate synthase	716533
Rib3	Saccharomyces cerevisiae	-	-	674407
RibA	Bacillus subtilis	-	-	675226
ribA2	Mycobacterium tuberculosis	A5U2B7	gene name, bi-bifunctional enzyme with DHBPS and GTPCH-II domains at N- and C-termini, respectively	716058
ribB	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	gene name	716877
L-3,4-dihydroxy-2-butanone-4-phosphate synthase	Meyerozyma guilliermondii	-	-	674401
additional information	Bacillus subtilis	-	cf. EC 3.5.4.25	675226

CAS REGISTRY NUMBER	COMMENTARY
No entries in this field

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Bacillus subtilis	gene ribA	675226	-	-
Candida albicans	-	690233	Q5A3V6	UniProt
Candida albicans	wild-type enzyme; ATCC 10231D, orf 6.2440	675342	Q5A3V6	UniProt
Escherichia coli	-	675576	-	-
Escherichia coli	-	676912, 677168	P0A7J0	Uniprot
Escherichia coli	gene ribB	673430	-	-
Escherichia coli	strain TG1	703578	-	-
Escherichia coli	strain W3110	671288	-	-
Escherichia coli K-12	gene ribB	675800	P0A7J0	SwissProt
Magnaporthe grisea	-	671037, 671958	-	-
Methanocaldococcus jannaschii	-	671038, 676912	-	-
Methanocaldococcus jannaschii	-	674408	Q60364	Uniprot
Methanocaldococcus jannaschii	orf MJ0055	674406	-	-
Meyerozyma guilliermondii	i.e. Pichia guilliermondii	674401, 674403	-	-
Mycobacterium tuberculosis	-	716058	A5U2B7	UniProt
Nicotiana benthamiana	-	716533	-	-
Saccharomyces cerevisiae	gene RIB3, wild-type strain W303-1A	674407	-	-
Salmonella enterica subsp. enterica serovar Typhimurium	-	716877	P66032	UniProt

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
malfunction	Nicotiana benthamiana	-	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
physiological function	Escherichia coli	-	the enzyme is involved in riboflavin biosynthesis. Up-regulation of DHBP synthase is evidenced as one of the first line strategies to cope with imbalance of energy production and vital adaptation	703578

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Bacillus subtilis	-	-	675226	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	-	-	671288, 673430, 675576	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	P0A7J0	-	676912	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	-	-	677168	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Saccharomyces cerevisiae	-	-	674407	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Methanocaldococcus jannaschii	-	-	674406, 676912	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Magnaporthe grisea	-	-	671037, 671958	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Nicotiana benthamiana	-	-	716533	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Candida albicans	Q5A3V6	-	675342	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Salmonella enterica subsp. enterica serovar Typhimurium	P66032	-	716877	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Meyerozyma guilliermondii	-	-	674401	product identification by NMR and CD spectroscopy	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli K-12	P0A7J0	substrate preparation, overview	675800	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Meyerozyma guilliermondii	-	a step in the formation of the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, from 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione requiring a phosphorylated 4-carbon intermediate, designated as compound X	674401	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Meyerozyma guilliermondii	-	a step in the formation of the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, from 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione requiring a phosphorylated 4-carbon intermediate, designated as compound X, analysis of the riboflavin biosynthetic pathway, overview	674403	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Methanocaldococcus jannaschii	-	DHBPS supplies the building blocks for the assembly of the xylene ring of the vitamin B2, riboflavin, all eight C atoms of the xylene moiety are derived from the product of the enzyme	671038	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Bacillus subtilis	-	rate-limiting step in riboflavin biosynthesis	675226	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	-	step in biosynthesis of vitamin B2, riboflavin	671288	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Methanocaldococcus jannaschii	Q60364	step in the biosynthesis of riboflavin, vitamin B2, ribulose 5-phosphate is converted into 3,4-dihydroxy-2-butanone 4-phosphate while its C4 atom is released as formate in a sequence of metal-dependent reactions	674408	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	-	the enzyme is important in riboflavin biosynthesis, overview	675576	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli K-12	P0A7J0	the enzyme is important in the riboflavin biosynthesis, the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, is formed by condensation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione (1) with 3,4-dihydroxy-2-butanone 4-phosphate, overview	675800	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Candida albicans	Q5A3V6	the enzyme is involved in riboflavin biosynthesis	675342	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	-	the enzyme is involved in the pathway of riboflavin biosynthesis	673430	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	P0A7J0	the enzyme is involved in the pathway of riboflavin biosynthesis	676912	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Methanocaldococcus jannaschii	-	the enzyme is involved in the pathway of riboflavin biosynthesis	676912	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	-	the enzyme is involved in the pathway of riboflavin biosynthesis, overview	677168	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Methanocaldococcus jannaschii	Q60364	a dimetal center is involved in substrate binding, structure-function relationship, overview	674408	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Meyerozyma guilliermondii	-	carbon atoms 1-3 of the enzyme product correspond to carbon atoms 1-3 of the substrate, whereas C-4 of the product stems from C-6 of the substrate. Carbon atom 4 of the substrate is released as formate together with the hydrogen atom attached to it. The skeletal rearrangement which leads to the loss of C-4 and the direct linkage between C-3 and C-6 of the substrate is an intramolecular reaction, the hydrogen atom at C-3 of the enzyme product is introduced from solvent water	674403	product identification by GC-MS	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Methanocaldococcus jannaschii	-	substrate binding structure involving a dimetal center, overview	671038	the enzyme converts ribulose 5-phosphate into 3,4-dihydroxy-2-butanone 4-phosphate, while its C4 atom is released as formate	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Methanocaldococcus jannaschii	-	the reaction involves an intramolecular skeletal rearrangement, NMR study	674406	-	-	?
D-ribulose 5-phosphate	formate + L-3,4-dihydroxybutan-2-one 4-phosphate		Candida albicans	Q5A3V6	-	690233	-	-	?
additional information	?	-	Bacillus subtilis	-	RibA is the rate limiting enzyme in an industrial riboflavin producing strain	675226	-	-	-
additional information	?	-	Saccharomyces cerevisiae	-	the enzyme is involved in the riboflavin biosynthetic pathway, but has a second unrelated function in expression of mitochondrial respiration	674407	-	-	-
additional information	?	-	Bacillus subtilis	-	RibA is a bifunctional enzyme possessing 3,4-dihydroxy-2-butanone 4-phosphate synthase activity located in the N-terminal half of the protein and GTP cyclohydrolase II activity, EC 3.5.4.25, of the C-terminal domain, overview	675226	-	-	-
additional information	?	-	Magnaporthe grisea	-	the position of the metal cofactors and the substrate�s phosphate group are further stabilized by an extensive hydrogen-bond and salt-bridge network, overview	671958	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Saccharomyces cerevisiae	-	-	674407	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Methanocaldococcus jannaschii	-	-	674406	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Magnaporthe grisea	-	-	671037, 671958	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Meyerozyma guilliermondii	-	a step in the formation of the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, from 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione requiring a phosphorylated 4-carbon intermediate, designated as compound X	674401	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Meyerozyma guilliermondii	-	a step in the formation of the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, from 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione requiring a phosphorylated 4-carbon intermediate, designated as compound X, analysis of the riboflavin biosynthetic pathway, overview	674403	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Methanocaldococcus jannaschii	-	DHBPS supplies the building blocks for the assembly of the xylene ring of the vitamin B2, riboflavin, all eight C atoms of the xylene moiety are derived from the product of the enzyme	671038	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Bacillus subtilis	-	rate-limiting step in riboflavin biosynthesis	675226	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	-	step in biosynthesis of vitamin B2, riboflavin	671288	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Methanocaldococcus jannaschii	Q60364	step in the biosynthesis of riboflavin, vitamin B2, ribulose 5-phosphate is converted into 3,4-dihydroxy-2-butanone 4-phosphate while its C4 atom is released as formate in a sequence of metal-dependent reactions	674408	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	-	the enzyme is important in riboflavin biosynthesis, overview	675576	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli K-12	P0A7J0	the enzyme is important in the riboflavin biosynthesis, the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, is formed by condensation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione (1) with 3,4-dihydroxy-2-butanone 4-phosphate, overview	675800	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Candida albicans	Q5A3V6	the enzyme is involved in riboflavin biosynthesis	675342	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	-	the enzyme is involved in the pathway of riboflavin biosynthesis	673430	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	P0A7J0	the enzyme is involved in the pathway of riboflavin biosynthesis	676912	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Methanocaldococcus jannaschii	-	the enzyme is involved in the pathway of riboflavin biosynthesis	676912	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxy-2-butanone-4-phosphate		Escherichia coli	-	the enzyme is involved in the pathway of riboflavin biosynthesis, overview	677168	-	-
D-ribulose 5-phosphate	formate + L-3,4-dihydroxybutan-2-one 4-phosphate		Candida albicans	Q5A3V6	-	690233	-	-
additional information	?	-	Bacillus subtilis	-	RibA is the rate limiting enzyme in an industrial riboflavin producing strain	675226	-	-
additional information	?	-	Saccharomyces cerevisiae	-	the enzyme is involved in the riboflavin biosynthetic pathway, but has a second unrelated function in expression of mitochondrial respiration	674407	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
additional information	Escherichia coli K-12	P0A7J0	no cofactor required	675800	-

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Ca2+	Methanocaldococcus jannaschii	-	Ca2+ binding requires the binding of the substrate, binding involves Glu204, Glu97, and Asn207	671038
Ca2+	Methanocaldococcus jannaschii	Q60364	binding structure, overview	674408
Ca2+	Candida albicans	Q5A3V6	not involved in catalysis, stabilize the enzyme	675342
Hg2+	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	moderate activity	716877
Mg2+	Escherichia coli	-	required, cannot be substituted by Ca2+, KM: 0.99 mM	671288
Mg2+	Magnaporthe grisea	-	required, two Mg2+ cations that bind to the oxygen substituents of the C2, C3, C4, and phosphate groups of the substrate, the side chains of Glu37 and His153, and water molecules	671958
Mg2+	Escherichia coli	-	required	673430
Mg2+	Meyerozyma guilliermondii	-	required for activity	674401
Mg2+	Meyerozyma guilliermondii	-	-	674403
Mg2+	Methanocaldococcus jannaschii	-	-	674406
Mg2+	Methanocaldococcus jannaschii	Q60364	binding structure, overview	674408
Mg2+	Bacillus subtilis	-	-	675226
Mg2+	Candida albicans	Q5A3V6	essential for activity	675342
Mg2+	Escherichia coli	-	required for activity	675576, 677168
Mg2+	Escherichia coli K-12	P0A7J0	required	675800
Mg2+	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	highest activity	716877
Ni2+	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	moderate activity	716877
sulfate	Magnaporthe grisea	-	binding structure at the active site, overview	671958
Zn2+	Methanocaldococcus jannaschii	-	bound at His164, binding involves His206, Glu132, and Glu128	671038
Zn2+	Magnaporthe grisea	-	binding structure, overview	671958
Zn2+	Methanocaldococcus jannaschii	Q60364	binding structure, overview	674408
Zn2+	Candida albicans	Q5A3V6	not involved in catalysis, stabilize the enzyme	675342
Mn2+	Magnaporthe grisea	-	binding structure, overview	671958
additional information	Methanocaldococcus jannaschii	-	substrate binding structure involving a dimetal center, overview	671038
additional information	Magnaporthe grisea	-	the position of the metal cofactors and the substrate�s phosphate group are further stabilized by an extensive hydrogen-bond and salt-bridge network, overview	671958
additional information	Methanocaldococcus jannaschii	Q60364	the enzyme depends on divalent metal ions, a dimetal center is involved in substrate binding	674408

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
EDTA	Meyerozyma guilliermondii	-	complete inhibition, reversible by Mg2+	674401	2D-image
EDTA	Bacillus subtilis	-	-	675226	2D-image
EDTA	Escherichia coli K-12	P0A7J0	complete inhibition	675800	2D-image

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.116	-	D-ribulose 5-phosphate	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	37�C, pH 7.5, Vmax: 199 nmol/min/mg	716877	2D-image

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
0.152	-	Escherichia coli	-	purified recombinant enzyme	673430
0.174	-	Methanocaldococcus jannaschii	-	purified enzyme	674406
0.283	-	Escherichia coli K-12	P0A7J0	purified recombinant enzyme, assay method development, overview	675800
0.332	-	Candida albicans	Q5A3V6	purified recombinant enzyme	675342
14	-	Meyerozyma guilliermondii	-	purified enzyme	674401
additional information	-	Escherichia coli	-	development of a spectrophotometric/colorimetric assay method, overview	671288

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7	-	Meyerozyma guilliermondii	-	assay at	674403
7.5	7.7	Methanocaldococcus jannaschii	-	assay at	674406
7.5	-	Escherichia coli	-	assay at	671288
7.5	-	Meyerozyma guilliermondii	-	assay at	674401
7.5	-	Candida albicans	Q5A3V6	assay at	675342
7.5	-	Escherichia coli K-12	P0A7J0	assay at	675800
7.5	-	Mycobacterium tuberculosis	A5U2B7	assay at, maximal activity	716058
7.5	-	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	assay at	716877
7.8	-	Escherichia coli	-	assay at	675576
8	-	Bacillus subtilis	-	assay at	675226
8	-	Nicotiana benthamiana	-	assay at	716533

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
5	9	Mycobacterium tuberculosis	A5U2B7	enzyme loses activity below pH 5.0 and above pH 9.0	716058
5	-	Mycobacterium tuberculosis	A5U2B7	below pH 5.0 enzyme forms an inactive monomer in solution. The functional activity of Mtb-DHBPS and its dimeric state can be restored by increasing the pH between 6.0 and 9.0	716058

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
25	-	Escherichia coli	-	assay at	671288, 675576
37	-	Meyerozyma guilliermondii	-	assay at	674401, 674403
37	-	Methanocaldococcus jannaschii	-	assay at	674406
37	-	Bacillus subtilis	-	assay at	675226
37	-	Candida albicans	Q5A3V6	assay at	675342
37	-	Escherichia coli K-12	P0A7J0	assay at	675800
37	-	Mycobacterium tuberculosis	A5U2B7	assay at	716058
37	-	Nicotiana benthamiana	-	assay at	716533
37	-	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	assay at	716877

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
4.8	-	Escherichia coli	-	calculated from sequence	703578

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
No entries in this field

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
cytosol	Saccharomyces cerevisiae	-	mainly	5829	674407
mitochondrion	Saccharomyces cerevisiae	-	in the intermembrane space, possibly associated with the outer membrane, minor enzyme portion	5739	674407
additional information	Saccharomyces cerevisiae	-	subcellular localization analysis, overview	-	674407

PDB	SCOP	CATH	ORGANISM
3mgz, download	SCOP (3mgz)	CATH (3mgz)	Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
3mio, download	SCOP (3mio)	CATH (3mio)	Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
3mk5, download	SCOP (3mk5)	CATH (3mk5)	Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
3lqu, download	SCOP (3lqu)	CATH (3lqu)	Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
3lrj, download	SCOP (3lrj)	CATH (3lrj)	Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
3ls6, download	SCOP (3ls6)	CATH (3ls6)	Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
3h07, download	SCOP (3h07)	CATH (3h07)	Yersinia pestis

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
23310	-	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	calculated from cDNA	716877
23640	-	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	MALDI	716877
27860	-	Escherichia coli	-	mass spectrometry	703578
30000	-	Meyerozyma guilliermondii	-	gel filtration	674401
41000	-	Candida albicans	Q5A3V6	recombinant enzyme, analytical ultracentrifugation, hydrodynamic studies	675342
44800	-	Escherichia coli	-	recombinant enzyme, analytical ultracentrifugation at 37�C	673430
46300	-	Escherichia coli	-	recombinant enzyme, hydrodynamic analysis, NMR structure study, analytical ultracentrifugation at 4�C, overview	673430
47000	-	Escherichia coli, Methanocaldococcus jannaschii	-	-	676912
50000	-	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	gel filtration, dimer in solution	716877
51600	-	Methanocaldococcus jannaschii	-	recombinant enzyme, analytical ultrafiltration	674406

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
?	Escherichia coli	-	x * 23177, mass spectrometry	671288
?	Saccharomyces cerevisiae	-	x * 28000, SDS-PAGE, x * 22500, about, sequence calculation	674407
?	Escherichia coli K-12	P0A7J0	x * 23251, recombinant enzyme, mass spectrometry	675800
dimer	Methanocaldococcus jannaschii	-	enzyme mutant H147S, crystal structure	671038
dimer	Magnaporthe grisea	-	determination of the active sites in the homodimer, crystal structure, overview	671958
dimer	Escherichia coli	-	2 * 23000, SDS-PAGE, hydrodynamic analysis, NMR structure study, 2 * 23351, mass spectrometry	673430
dimer	Methanocaldococcus jannaschii	-	2 * 25799, recombinant enzyme, mass spectrometry and SDS-PAGE	674406
dimer	Candida albicans	Q5A3V6	2 * 22530, mass spectrometry, 2 * 22658, full-length enzyme, sequence calculation	675342
dimer	Escherichia coli, Methanocaldococcus jannaschii	-	three-dimensional structure, structure-activity relationship study using NMR spectroscopy, residue-specific isotope labeling, and protein deuteration strategies, solution structure, overview	676912
homodimer	Mycobacterium tuberculosis	A5U2B7	between pH 6.0-9.0, gel filtration	716058
homodimer	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	gel filtration, 2 * 23310	716877
monomer	Meyerozyma guilliermondii	-	1 * 24000, SDS-PAGE	674401
monomer	Mycobacterium tuberculosis	A5U2B7	below pH 5.0 enzyme forms an inactive monomer in solution, gel filtration	716058
additional information	Escherichia coli	-	hydrodynamic analysis, NMR structure study, isotope labeling, the homodimeric protein obeys strict C2 symmetry, overview	673430
additional information	Methanocaldococcus jannaschii	Q60364	structure-function relationship, overview	674408
additional information	Candida albicans	Q5A3V6	the enzyme possesses an essential acidic active-site loop, active site structure, structure comparisons, overview	675342
additional information	Escherichia coli	-	structure determination and analysis of functions of single residues, overview, dimer interface structure, localization of the active site, sequence and structure comparison	677168

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
purified recombinant apoenzyme in complex with the substrate ribulose 5-phosphate, sitting drop vapour diffusion method, 0.003 ml of 17-34 mg/ml protein in 50 mM Tris-HCl, pH 7.5, is mixed with 0.001 ml of reservoir solution containing 85 mM sodium citrate, pH 5.0, and 17% PEG 8000, with or without 5 mM EDTA, equilibration against 0.3 ml reservoir solution, 0.003 ml of the complex solution is mixed with 0.001 ml of 90 mM Mes/NaOH, pH 6.0, containing 18% PEG 8000, addition of 2 mM D-ribulose 5-phosphate, 20�C, X-ray diffraction structure determination and analysis at 1.6-1.7 A resolution, molecular replacement, modelling	Candida albicans	Q5A3V6	675342
reinterpretation of the space-group symmetry is reported for two crystal structures, PDB codes 1tks and 1tku	Candida albicans	Q5A3V6	690233
purified recombinant enzyme, hanging drop vapour diffusion method at room temperature, 4-5 days, 0.0022 ml of protein solution containing 24 mg/ml protein in 50mMTris-HCl pH 7.5, is mixed with 0.0007 ml of precipitating well solution containing 3 M CsCl, 3 M Cs-formate, 20 mM Bis-Tris-propane-NaOH, pH 6.9, or 6 M sodium formate, 25 mM HEPES-NaOH, pH 7.0, labeling with 1.5 mM Au(CN)2, X-ray diffraction structure determination and analysis at 1.4-2.4 A resolution, multiwavelength anomalous diffraction	Escherichia coli	-	677168
purified recombinant enzyme, crystallization of different enzyme complexes: E-SO42-, E-SO42-Mg2+, E-SO42-Mn2+, E-SO42-Mn2+-glycerol, and E-SO42-Zn2+ complexes with X-ray diffraction structure determination and and analysis at resolutions that extend to 1.55 A, 0.98 A, 1.60 A, 1.16 A, and 1.00 A, respectively, divalent cation-free enzyme from 24-30% PEG 5000 monomethyl ether, 0.2 M Li2SO4, and 0.1 M MES-NaOH, pH 6.0-6.5, by the hanging drop vapor diffusion method, to prepare divalent cation-containing crystals, 200 mM MgCl2, 200 mM MnCl2, or 200 mM zinc acetate are added to the crystals for 8-16 h in soaking solutions of the well solutions omitting Li2SO4 and 4% higher in the concentration of PEG 5000 monomethyl ether	Magnaporthe grisea	-	671958
purified recombinnat enzyme divalent cation free, soaked in Zn2+ or soaked in Mg2+, hanging drop vapor diffusion method, room temperature, 0.001 ml of 7 mg/ml protein in 50 mM Tris-HCl, pH 7.5, is mixed with 0.001 ml well solution containing 24-30% PEG monomethyl ether, 0.2 M Li2SO4, and 0.1 M MES-NaOH, pH 6.0-6.5, 1 week-3 months, rectangular plates, X-ray diffraction structure determination and analysis at 1.5 A, 1.0 A, and 1.8 A resolution, respectively	Magnaporthe grisea	-	671037
purified enzyme mutant H147S in complex with substrate ribulose 5-phosphate, monoclinic crystal form, X-ray diffraction structure determination and analysis at 1.55-1.7 A resolution	Methanocaldococcus jannaschii	-	671038
three crystal structures of Mtb-DHBPS domain in complex with phosphate and glycerol at pH 6.0, with sulfate at pH 4.0 and with zinc and sulfate at pH 4.0 are determined at 1.8, 2.06 and 2.06 A resolution, respectively	Mycobacterium tuberculosis	A5U2B7	716058
the crystal structures of Salmonella DHBPS in complex with sulfate, D-ribulose 5-phosphate and sulfate-zinc ion is determined at a resolution of 2.80, 2.52, and 1.86 A, respectively. Analysis of these crystal structures reveals that the acidic loop (residues 34-39) responsible for the acid-base catalysis is disordered in the absence of substrate or metal ion at the active site. Upon binding either substrate or sulfate and metal ions, the acidic loop becomes stabilized, adopts a closed conformation and interacts with the substrate	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	716877

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
recombinant enzyme, expressed from the synthetic gene in Escherichia coli, to homogeneity by hydrophobic interaction chromatography, ultrafiltration, and gel filtration	Candida albicans	Q5A3V6	675342
recombinant enzyme from strain Bl21(DE3) by hydrophobic interaction and anion exchange chromatography, and ultrafiltration	Escherichia coli	-	671288
recombinant enzyme from strain M15 by anion exchange chromatography and gel filtration	Escherichia coli	-	673430
native enzyme by anion and cation exchange chromatography, hydroxyapatite chromatography, and gel filtration, to homogeneity, recombinant enzyme from the overexpressing strain by anion exchange chromatography and gel filtration	Escherichia coli K-12	P0A7J0	675800
recombinant enzyme from Escherichia coli strain BL21(DE3) by anion exchange and hydroxylapatite chromatography, followed by ultrafiltration	Magnaporthe grisea	-	671037
recombinant wild-type and mutant enzymes from Escherichia coli by hydrophobic interaction and hydroxyapatite chromatography, and ultrafiltration	Methanocaldococcus jannaschii	-	674406
native enzyme to homogeneity, by anion and cation exchange chromatography, hydroxyapatite chromatography, and gel filtration	Meyerozyma guilliermondii	-	674401
using Ni-NTA chromatography	Mycobacterium tuberculosis	A5U2B7	716058
using Ni-NTA chromatography	Nicotiana benthamiana	-	716533
using Ni-NTA chromatography	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	716877

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
overexpression in strain 1012 by gene insertion in the sacB locus	Bacillus subtilis	-	675226
functional expression of the synthetic gene in Escherichia coli strains XL1-Blue and M15	Candida albicans	Q5A3V6	675342
-	Escherichia coli	-	676912
gene ribB, DNA determination and analysis, overexpression in strain M15	Escherichia coli	-	673430
subcloning in strain DH5alpha, expression in strain BL21(DE3)	Escherichia coli	-	671288
gene ribB, overexpression in an rib-defective mutant strain	Escherichia coli K-12	P0A7J0	675800
cloning by functional complementation of an Escherichia coli DS knockout mutant, expression in Escherichia coli strain BL21(DE3)	Magnaporthe grisea	-	671037
expression in Escherichia coli	Magnaporthe grisea	-	671958
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli strains XL-1 Blue and M15	Methanocaldococcus jannaschii	-	674406
expression in Escherichia coli	Methanocaldococcus jannaschii	-	676912
expressed in Escherichia coli	Mycobacterium tuberculosis	A5U2B7	716058
expressed in Escherichia coli	Nicotiana benthamiana	-	716533
gene RIB3, expression of the wild-type gene restores the ability to respire in the aE280/U1 pet mutant A137T of Saccharomyces cerevisiae, which is partially deficient in cytochromes a, a3, and cytochrome b	Saccharomyces cerevisiae	-	674407
expressed in Escherichia coli as a His-tagged fusion protein	Salmonella enterica subsp. enterica serovar Typhimurium	P66032	716877

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
increase of 3,4-dihydroxy-2-butanone 4-phosphate synthase upon exposure to Cd2+	Escherichia coli	-	703578

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
C59A	Candida albicans	Q5A3V6	site-directed mutagenesis, the mutant shows 70% of wild-type enzyme activity	675342
D92A	Candida albicans	Q5A3V6	site-directed mutagenesis, inactive mutant	675342
E166A	Candida albicans	Q5A3V6	site-directed mutagenesis, inactive mutant	675342
Q181R/Q183R	Candida albicans	Q5A3V6	site-directed mutagenesis, construction of a synthetic gene, derived from orf 6.2440, with nucleotide exchanges at positions 414, 426, 477, 480, and 581	675342
Y87A	Candida albicans	Q5A3V6	site-directed mutagenesis, the mutant shows 2% of wild-type enzyme activity	675342
D21E	Methanocaldococcus jannaschii	-	site-directed mutagenesis, inactive mutant	674406
D21N	Methanocaldococcus jannaschii	-	site-directed mutagenesis, inactive mutant	674406
D30E	Methanocaldococcus jannaschii	-	site-directed mutagenesis, inactive mutant	674406
E185D	Methanocaldococcus jannaschii	-	site-directed mutagenesis, inactive mutant	674406
E185X	Methanocaldococcus jannaschii	Q60364	site-directed mutagenesis, inactive mutant	674408
E26D	Methanocaldococcus jannaschii	-	site-directed mutagenesis, inactive mutant	674406
E26Q	Methanocaldococcus jannaschii	-	site-directed mutagenesis, inactive mutant	674406
E28D	Methanocaldococcus jannaschii	-	site-directed mutagenesis, inactive mutant	674406
H147S	Methanocaldococcus jannaschii	-	site-directed mutagenesis, the mutant shows about 10% of wild-type enzyme activity, crystal structure determination with bound substrate	671038
H147S	Methanocaldococcus jannaschii	Q60364	site-directed mutagenesis, the mutant enzyme shows about 10% of the wild-type enzyme activity	674408
H164N	Methanocaldococcus jannaschii	-	site-directed mutagenesis, inactive mutant	674406
E154D	Nicotiana benthamiana	-	DBPS activity is abolished	716533
additional information	Bacillus subtilis	-	an additional single copy of the ribA gene introduced into the sacBlocus of the riboflavin production strain and constitutive expression from the medium strength vegI promoter leads to improved riboflavin titers and yields of riboflavin on glucose of up to 25%, strain VB2XL1, both enzymatic activities of RibA, the 3,4-dihydroxy-2-butanone 4-phosphate synthase activity located in the N-terminal half of the protein and the GTP cyclohydrolase II activity of the C-terminal domain, are necessary for the improved riboflavin productivity, method, overview	675226
A137T	Saccharomyces cerevisiae	-	naturally occuring Rib3 mutant which is partially deficient in cytochromes a, a3, and cytochrome b, the respiratory defect elicited by this mutation cannot be explained by a flavin insufficiency based on the following evidence: 1. growth of the aE280/U1 on respiratory substrates is not rescued by exogenous riboflavin, 2. the levels of flavin nucleotides are not significantly different in the mutant and wild type, phenotype, overview	674407
additional information	Saccharomyces cerevisiae	-	construction of RIB3 disruption mutants, restoration by riboflavin of growth of a rib3 deletion mutant on glucose but not glycerol/ethanol, phenotype, overview	674407

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
synthesis	Bacillus subtilis	-	the enzyme is essential for industrial riboflavin production by Bacillus subtilis overproducing strains, overview	675226
drug development	Candida albicans	Q5A3V6	the ezyme is a potential anti-infective target in the pathogenic yeast	675342
drug development	Escherichia coli	-	the enzyme is a target in antimicrobial inhibitor development, structure-based inhibitor design	671288
drug development	Escherichia coli	-	the enzyme is an attractive target for antibiotics, design of mechanism-based inhibitors	676912

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
671037	Liao, D.I.; Viitanen, P.V.; Jordan, D.B.	Cloning, expression, purification and crystallization of dihydroxybutanone phosphate synthase from Magnaporthe grisea	Acta Crystallogr. Sect. D	56	1495-1497	2000	Magnaporthe grisea	PubMed
671038	Steinbacher, S.; Schiffmann, S.; Bacher, A.; Fischer, M.	Metal sites in 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with the substrate ribulose 5-phosphate	Acta Crystallogr. Sect. D	60	1338-1340	2004	Methanocaldococcus jannaschii	PubMed
671288	Picollelli, M.A.; Viitanen, P.V.; Jordan, D.B.	Spectrophotometric determination of 3,4-dihydroxy-2-butanone-4-phosphate synthase activity	Anal. Biochem.	287	347-349	2000	Escherichia coli	PubMed
671958	Liao, D.I.; Zheng, Y.J.; Viitanen, P.V.; Jordan, D.B.	Structural definition of the active site and catalytic mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase	Biochemistry	41	1795-1806	2002	Magnaporthe grisea	PubMed
673430	Richter, G.; Kelly, M.; Krieger, C.; Yu, Y.; Bermel, W.; Karlsson, G.; Bacher, A.; Oschkinat, H.	NMR studies on the 46-kDa dimeric protein, 3,4-dihydroxy-2-butanone 4-phosphate synthase, using 2H, 13C, and 15N-labelling	Eur. J. Biochem.	261	57-65	1999	Escherichia coli	PubMed
674401	Volk, R.; Bacher, A.	Studies on the 4-carbon precursor in the biosynthesis of riboflavin. Purification and properties of L-3,4-dihydroxy-2-butanone-4-phosphate synthase	J. Biol. Chem.	265	19479-19485	1990	Meyerozyma guilliermondii	PubMed
674403	Volk, R.; Bacher, A.	Biosynthesis of riboflavin. Studies on the mechanism of L-3,4-dihydroxy-2-butanone 4-phosphate synthase	J. Biol. Chem.	266	20610-20618	1991	Meyerozyma guilliermondii	PubMed
674406	Fischer, M.; Romisch, W.; Schiffmann, S.; Kelly, M.; Oschkinat, H.; Steinbacher, S.; Huber, R.; Eisenreich, W.; Richter, G.; Bacher, A.	Biosynthesis of riboflavin in archaea studies on the mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase of Methanococcus jannaschii	J. Biol. Chem.	277	41410-41416	2002	Methanocaldococcus jannaschii	PubMed
674407	Jin, C.; Barrientos, A.; Tzagoloff, A.	Yeast dihydroxybutanone phosphate synthase, an enzyme of the riboflavin biosynthetic pathway, has a second unrelated function in expression of mitochondrial respiration	J. Biol. Chem.	278	14698-14703	2003	Saccharomyces cerevisiae	PubMed
674408	Steinbacher, S.; Schiffmann, S.; Richter, G.; Huber, R.; Bacher, A.; Fischer, M.	Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with divalent metal ions and the substrate ribulose 5-phosphate: implications for the catalytic mechanism	J. Biol. Chem.	278	42256-42265	2003	Methanocaldococcus jannaschii	PubMed
675226	Huembelin, M.; Griesser, V.; Keller, T.; Schurter, W.; Haiker, M.; Hohmann, H.P.; Ritz, H.; Richter, G.; Bacher, A.; Van Loon, A.P.G.M.	GTP cyclohydrolase II and 3,4-dihydroxy-2-butanone 4-phosphate synthase are rate-limiting enzymes in riboflavin synthesis of an industrial Bacillus subtilis strain used for riboflavin production	J. Indust. Microbiol. Biotechnol.	22	1-7	1999	Bacillus subtilis	-
675342	Echt, S.; Bauer, S.; Steinbacher, S.; Huber, R.; Bacher, A.; Fischer, M.	Potential anti-infective targets in pathogenic yeasts: structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans	J. Mol. Biol.	341	1085-1096	2004	Candida albicans	PubMed
675576	Goetze, E.; Kis, K.; Eisenreich, W.; Yamauchi, N.; Kakinuma, K.; Bacher, A.	Biosynthesis of riboflavin. Stereochemistry of the 3,4-dihydroxy-2-butanone 4-phosphate synthase reaction	J. Org. Chem.	63	6456-6457	1998	Escherichia coli	-
675800	Richter, G.; Krieger, C.; Volk, R.; Kis, K.; Ritz, H.; Gotze, E.; Bacher, A.	Biosynthesis of riboflavin: 3,4-dihydroxy-2-butanone-4-phosphate synthase	Methods Enzymol.	280	374-382	1997	Escherichia coli K-12	PubMed
676912	Kelly, M.J.; Ball, L.J.; Krieger, C.; Yu, Y.; Fischer, M.; Schiffmann, S.; Schmieder, P.; Kuhne, R.; Bermel, W.; Bacher, A.; Richter, G.; Oschkinat, H.	The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site	Proc. Natl. Acad. Sci. USA	98	13025-13030	2001	Escherichia coli, Methanocaldococcus jannaschii	PubMed
677168	Liao, D.I.; Calabrese, J.C.; Wawrzak, Z.; Viitanen, P.V.; Jordan, D.B.	Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis	Structure	9	11-18	2001	Escherichia coli	PubMed
690233	Le Trong, I.; Stenkamp, R.E.	Alternative models for two crystal structures of Candida albicans 3,4-dihydroxy-2-butanone 4-phosphate synthase	Acta Crystallogr. Sect. D	64	219-220	2008	Candida albicans	PubMed
703578	Isarankura-Na-Ayudhya, P.; Isarankura-Na-Ayudhya, C.; Treeratanapaiboon, L.; Kasikun, K.; Thipkeaw, K.; Prachayasittikul, V.	Proteomic profiling of Escherichia coli in response to heavy metals stress	Eur. J. Sci. Res.	25	679-688	2009	Escherichia coli	-
716058	Singh, M.; Kumar, P.; Karthikeyan, S.	Structural basis for pH dependent monomer-dimer transition of 3,4-dihydroxy 2-butanone-4-phosphate synthase domain from Mycobacterium tuberculosis	J. Struct. Biol.	174	374-384	2011	Mycobacterium tuberculosis	PubMed
716533	Asai, S.; Mase, K.; Yoshioka, H.	A key enzyme for flavin synthesis is required for nitric oxide and reactive oxygen species production in disease resistance	Plant J.	62	911-924	2010	Nicotiana benthamiana	PubMed
716877	Kumar, P.; Singh, M.; Gautam, R.; Karthikeyan, S.	Potential anti-bacterial drug target: structural characterization of 3,4-dihydroxy-2-butanone-4-phosphate synthase from Salmonella typhimurium LT2	Proteins	78	3292-3303	2010	Salmonella enterica subsp. enterica serovar Typhimurium	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 4.1.99.12)

NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM

IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

SYSTERS

Protein Mutant Database

InterPro (database of protein families, domains and functional sites)

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