EC 2.5.1.3
- Thiamine phosphate synthase
IntEnz Enzyme Nomenclature
EC 2.5.1.3
Names
Accepted name:
thiamine phosphate synthase
Other
names:
TMP-PPase
thiamine monophosphate pyrophosphorylase
thiamine phosphate pyrophosphorylase
thiamine-phosphate pyrophosphorylase
TMP pyrophosphorylase
thiamine-phosphate synthase
TMP diphosphorylase
thiamine-phosphate diphosphorylase
thiE (gene name)
TH1 (gene name)
THI6 (gene name)
2-methyl-4-amino-5-hydroxymethylpyrimidine-diphosphate:4-methyl-5-(2-phosphoethyl)thiazole 2-methyl-4-aminopyrimidine-5-methenyltransferase
Systematic name:
4-amino-2-methyl-5-diphosphomethylpyrimidine:2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate 4-amino-2-methylpyrimidine-5-methenyltransferase (decarboxylating)
Reactions
-
(1)
4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate = diphosphate + thiamine phosphate + CO2
-
(2)
4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = diphosphate + thiamine phosphate + CO2
-
(3)
4-amino-2-methyl-5-diphosphomethylpyrimidine + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate
Comments:
The enzyme catalyses the penultimate reaction in thiamine de novo biosynthesis, condensing the pyrimidine and thiazole components. The enzyme is thought to accept the product of EC 2.8.1.10, thiazole synthase, as its substrate. However, it has been shown that in some bacteria, such as Bacillus subtilis, an additional enzyme, thiazole tautomerase (EC 5.3.99.10) converts that compound into its tautomer 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate, and that it is the latter that serves as the substrate for the synthase. In addition to this activity, the enzyme participates in a salvage pathway, acting on 4-methyl-5-(2-phosphono-oxyethyl)thiazole, which is produced from thiamine degradation products. In yeast this activity is found in a bifunctional enzyme (THI6) and in the plant Arabidopsis thaliana the activity is part of a trifunctional enzyme (TH1).
Links to other databases
CAS Registry Number:
9030-30-2
THI6_SCHPO
THI6_YEAST
THIDN_METJA
THIDN_THEMA
THIE1_AQUAE
THIE1_STRPN
THIE1_STRR6
THIE2_AQUAE
THIE2_STRPN
THIE2_STRR6
THIEC_BIFLO
THIED_COREF
THIED_CORGL
THIED_GEOSL
THIE_ACIC1
THIE_ACIF2
THIE_ACIF5
THIE_ACTP7
THIE_ACTSZ
THIE_AGRFC
THIE_ALCBS
THIE_ALKHC
THIE_ALKMQ
THIE_ALKOO
THIE_ANADE
THIE_ANOFW
THIE_ARCFU
THIE_AROAE
THIE_ARTS2
THIE_AZOC5
THIE_AZOSB
THIE_AZOVD
THIE_BACAA
THIE_BACAC
THIE_BACAH
THIE_BACAN
THIE_BACC0
THIE_BACC1
THIE_BACC3
THIE_BACC4
THIE_BACC7
THIE_BACCN
THIE_BACCQ
THIE_BACCR
THIE_BACCZ
THIE_BACFN
THIE_BACFR
THIE_BACHK
THIE_BACLD
THIE_BACMK
THIE_BACP2
THIE_BACSK
THIE_BACSU
THIE_BACTN
THIE_BACVZ
THIE_BORA1
THIE_BORBR
THIE_BORPA
THIE_BORPE
THIE_CALBD
THIE_CALMQ
THIE_CALS4
THIE_CALS8
THIE_CAMJ8
THIE_CAMJE
THIE_CAMJJ
THIE_CAMJR
THIE_CAUSK
THIE_CHLAA
THIE_CHLAB
THIE_CHLCV
THIE_CHLL2
THIE_CHLL3
THIE_CHLP8
THIE_CHLPD
THIE_CHLPM
THIE_CHLTE
THIE_CHRVO
THIE_CITK8
THIE_CLOAB
THIE_CLOB1
THIE_CLOB6
THIE_CLOB8
THIE_CLOBA
THIE_CLOBB
THIE_CLOBH
THIE_CLOBJ
THIE_CLOBK
THIE_CLOBL
THIE_CLOBM
THIE_CLOD6
THIE_CLONN
THIE_CLOP1
THIE_CLOPE
THIE_CLOPS
THIE_CLOTE
THIE_COPPD
THIE_COREF
THIE_CORJK
THIE_CROS8
THIE_DECAR
THIE_DEIGD
THIE_DEIRA
THIE_DESHD
THIE_DESHY
THIE_DESMR
THIE_DICT6
THIE_DICTD
THIE_ECO24
THIE_ECO57
THIE_ECO5E
THIE_ECOHS
THIE_ECOK1
THIE_ECOL5
THIE_ECOL6
THIE_ECOLC
THIE_ECOLI
THIE_ECOSE
THIE_ECOUT
THIE_ENT38
THIE_ENTFA
THIE_ERYLH
THIE_FLAJ1
THIE_FLAPJ
THIE_FUSNN
THIE_GEOKA
THIE_GEOSL
THIE_GEOTN
THIE_GLOVI
THIE_HAEI8
THIE_HAEIE
THIE_HAEIG
THIE_HAEIN
THIE_HAES1
THIE_HALHL
THIE_HALMA
THIE_HALWD
THIE_HELPH
THIE_HELPJ
THIE_HELPS
THIE_HELPY
THIE_HERA2
THIE_HYDS0
THIE_HYPNA
THIE_JANMA
THIE_KINRD
THIE_KLEP7
THIE_KORVE
THIE_LACCB
THIE_LACLA
THIE_LACLM
THIE_LACLS
THIE_LACP3
THIE_LACPL
THIE_LARHH
THIE_LATSS
THIE_LAWIP
THIE_LEPBA
THIE_LEPBP
THIE_LEUCK
THIE_LEVBA
THIE_LIMF3
THIE_LIMRD
THIE_LIMRJ
THIE_LISIN
THIE_LISMC
THIE_LISMF
THIE_LISMH
THIE_LISMO
THIE_LISW6
THIE_LYSSC
THIE_MANSM
THIE_MARN8
THIE_METAC
THIE_METAR
THIE_METB6
THIE_METBF
THIE_METCA
THIE_METFK
THIE_METHJ
THIE_METM5
THIE_METM6
THIE_METM7
THIE_METMA
THIE_METMJ
THIE_METMP
THIE_METS3
THIE_METVS
THIE_MOOTA
THIE_MYCA1
THIE_MYCBO
THIE_MYCBP
THIE_MYCGI
THIE_MYCLB
THIE_MYCLE
THIE_MYCMM
THIE_MYCPA
THIE_MYCS2
THIE_MYCSJ
THIE_MYCSK
THIE_MYCSS
THIE_MYCTA
THIE_MYCTO
THIE_MYCTU
THIE_MYCUA
THIE_MYCVP
THIE_MYXXD
THIE_NATPD
THIE_NEIG1
THIE_NEIMA
THIE_NEIMB
THIE_NITEC
THIE_NITEU
THIE_NITMU
THIE_NITOC
THIE_NOCFA
THIE_NOSP7
THIE_NOSS1
THIE_OCEIH
THIE_PARMW
THIE_PASMU
THIE_PECAS
THIE_PEDPA
THIE_PELTS
THIE_PELUB
THIE_PERMH
THIE_PHOLL
THIE_PHOV8
THIE_PICTO
THIE_PROM3
THIE_PROMA
THIE_PROMH
THIE_PROMM
THIE_PROMP
THIE_PROMS
THIE_PSE14
THIE_PSEA7
THIE_PSEA8
THIE_PSEAB
THIE_PSEAE
THIE_PSEE4
THIE_PSEF5
THIE_PSEFS
THIE_PSEMY
THIE_PSEP1
THIE_PSEPF
THIE_PSEPG
THIE_PSEPK
THIE_PSEPW
THIE_PSESM
THIE_PSEU2
THIE_PSEU5
THIE_PSYWF
THIE_PYRAB
THIE_PYRFU
THIE_PYRHO
THIE_RHIEC
THIE_RHOBA
THIE_RHOCS
THIE_RHOFT
THIE_ROSCS
THIE_ROSS1
THIE_RUMCH
THIE_SACD2
THIE_SACEN
THIE_SALA4
THIE_SALAI
THIE_SALAR
THIE_SALCH
THIE_SALDC
THIE_SALEP
THIE_SALG2
THIE_SALHS
THIE_SALNS
THIE_SALPA
THIE_SALPB
THIE_SALPK
THIE_SALRD
THIE_SALSV
THIE_SALTI
THIE_SALTO
THIE_SALTY
THIE_SERP5
THIE_SHIB3
THIE_SHIBS
THIE_SHIDS
THIE_SHIF8
THIE_SHIFL
THIE_SHISS
THIE_STAA1
THIE_STAA2
THIE_STAA3
THIE_STAA8
THIE_STAA9
THIE_STAAB
THIE_STAAC
THIE_STAAE
THIE_STAAM
THIE_STAAN
THIE_STAAR
THIE_STAAS
THIE_STAAW
THIE_STACT
THIE_STAEQ
THIE_STAES
THIE_STAHJ
THIE_STAS1
THIE_STRA1
THIE_STRA3
THIE_STRA5
THIE_STRAW
THIE_STRCO
THIE_STRS2
THIE_SYNPW
THIE_SYNS3
THIE_SYNSC
THIE_SYNWW
THIE_SYNY3
THIE_THEAC
THIE_THEFY
THIE_THET2
THIE_THET8
THIE_THEVB
THIE_THEVO
THIE_THIDA
THIE_THISH
THIE_VIBCB
THIE_VIBPA
THIE_WOLSU
THIE_XANAC
THIE_XANC8
THIE_XANCP
THIE_XANP2
THIE_XYLFA
THIE_XYLFT
THIE_YERP3
THIE_YERPA
THIE_YERPE
THIE_YERPN
THIE_YERPP
THIE_YERPS
THIME_SYMTH
THIN_METTH
TPS1L_ARATH
TPS1_BRANA
TPS1_ORYSJ
References
-
Camiener, G.W. and Brown, G.M.
The biosynthesis of thiamine. 2. Fractionation of enzyme system and identification of thiazole monophosphate and thiamine monophosphate as intermediates.
J. Biol. Chem.
235
:
2411-2417
(1960).
[PMID:
13807175]
-
Leder, I.G.
The enzymatic synthesis of thiamine monophosphate.
J. Biol. Chem.
236
:
3066-3071
(1961).
[PMID:
14463407]
-
Kawasaki, Y.
Copurification of hydroxyethylthiazole kinase and thiamine-phosphate pyrophosphorylase of Saccharomyces cerevisiae: characterization of hydroxyethylthiazole kinase as a bifunctional enzyme in the thiamine biosynthetic pathway.
J. Bacteriol.
175
:
5153-5158
(1993).
[PMID:
8394314]
-
Backstrom, A.D., McMordie, R.A.S. and Begley, T.P.
Biosynthesis of thiamin I: the function of the thiE gene product.
J. Am. Chem. Soc.
117
:
2351-2352
(1995).
-
Chiu, H. J., Reddick, J. J., Begley, T. P., Ealick, S. E.
Crystal structure of thiamin phosphate synthase from Bacillus subtilis at 1.25 Å resolution.
Biochemistry
38
:
6460-6470
(1999).
[PMID:
10350464]
[EC 2.5.1.3 created 1965, modified 2015]