| | ENZYME: 1.1.1.153 |

Entry

EC 1.1.1.153                Enzyme

Name

sepiapterin reductase;
SR

Class

Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor

Sysname

7,8-dihydrobiopterin:NADP+ oxidoreductase

Reaction(IUBMB)

(1) 7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+ [RN:R02975];
(2) tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+ [RN:R08208]

Reaction(KEGG)

R02975 R08208;
(other) R01813 R04285

Substrate

7,8-dihydrobiopterin [CPD:C02953];
NADP+ [CPD:C00006];
tetrahydrobiopterin [CPD:C00272]

Product

sepiapterin [CPD:C00835];
NADPH [CPD:C00005];
H+ [CPD:C00080];
6-pyruvoyl-5,6,7,8-tetrahydropterin [CPD:C03684]

Comment

This enzyme catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 3.5.4.16 (GTP cyclohydrolase I) and EC 4.2.3.12 (6-pyruvoyltetrahydropterin synthase) [5].

Pathway

ec00790 | Folate biosynthesis
ec01100 | Metabolic pathways

Orthology

K00072 | sepiapterin reductase

Genes

HSA: | 6697(SPR)
PTR: | 470403(SPR)
PON: | 100445031
MCC: | 705317(SPR)
MMU: | 20751(Spr)
RNO: | 29270(Spr)
CFA: | 483118(SPR)
AML: | 100465478
BTA: | 533836(SPR)
SSC: | 100521367
ECB: | 100059420
MDO: | 100010091
OAA: | 100091653
GGA: | 425255(SPR)
MGP: | 100542371
XLA: | 380273(spr)
XTR: | 100145068(spr)
DRE: | 554136(spra)
BFO: | BRAFLDRAFT_208259 BRAFLDRAFT_85347 BRAFLDRAFT_87528 BRAFLDRAFT_99985
CIN: | 100180453 100183871
SPU: | 577750
DME: | Dmel_CG12116 Dmel_CG12117(Sptr)
DPO: | Dpse_GA11411
DAN: | Dana_GF22580 Dana_GF22581
DER: | Dere_GG19045 Dere_GG19046
DPE: | Dper_GL20245 Dper_GL20246
DSE: | Dsec_GM21301 Dsec_GM21323
DSI: | Dsim_GD16109 Dsim_GD16111
DWI: | Dwil_GK19889 Dwil_GK19890
DYA: | Dyak_GE17449 Dyak_GE17450
DGR: | Dgri_GH12504 Dgri_GH12505
DMO: | Dmoj_GI14857 Dmoj_GI14858
DVI: | Dvir_GJ19518
AGA: | AgaP_AGAP008000
AAG: | AaeL_AAEL001845
CQU: | CpipJ_CPIJ000511
AME: | 551857
NVI: | 100119617(NV10057)
TCA: | 662832
API: | 100162307
PHU: | Phum_PHUM366100
ISC: | IscW_ISCW002953
BMY: | Bm1_29970
NVE: | NEMVE_v1g161481
HMG: | 100198898
TAD: | TRIADDRAFT_58441
DDI: | DDB_G0290009(sr)
TGO: | TGME49_031920
PTI: | PHATRDRAFT_45294
TPS: | THAPSDRAFT_261572(SPR1)
PIF: | PITG_11445

Reference

1  [PMID:4401291]

Authors

Kato S.

Title

Sepiapterin reductase from horse liver: purification and properties of the enzyme.

Journal

Arch. Biochem. Biophys. 146 (1971) 202-14.

Organism

Rattus norvegicus [GN:rno], Equus caballus [GN:ecb]

Reference

2  [PMID:5969298]

Authors

Matsubara M, Katoh S, Akino M, Kaufman S.

Title

Sepiapterin reductase.

Journal

Biochim. Biophys. Acta. 122 (1966) 202-12.

Organism

Rattus norvegicus [GN:rno]

Reference

3  [PMID:7528005]

Authors

Werner ER, Schmid M, Werner-Felmayer G, Mayer B, Wachter H.

Title

Synthesis and characterization of 3H-labelled tetrahydrobiopterin.

Journal

Biochem. J. 304 ( Pt 1) (1994) 189-93.

Organism

Rattus norvegicus [GN:rno]

Reference

4  [PMID:10987137]

Authors

Kim YA, Chung HJ, Kim YJ, Choi YK, Hwang YK, Lee SW, Park YS.

Title

Characterization of recombinant Dictyostelium discoideum sepiapterin reductase expressed in E. coli.

Journal

Mol. Cells. 10 (2000) 405-10.

Organism

Dictyostelium discoideum [GN:ddi]

Reference

5  [PMID:16510994]

Authors

Supangat S, Choi YK, Park YS, Son D, Han CD, Lee KH.

Title

Expression, purification, crystallization and preliminary X-ray analysis of sepiapterin reductase from Chlorobium tepidum.

Journal

Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 61 (2005) 202-4.

Organism

Chlorobium tepidum

Reference

6  [PMID:15621425]

Authors

Choi YK, Jun SR, Cha EY, Park JS, Park YS.

Title

Sepiapterin reductases from Chlorobium tepidum and Chlorobium limicola catalyze the synthesis of L-threo-tetrahydrobiopterin from 6-pyruvoyltetrahydropterin.

Journal

FEMS. Microbiol. Lett. 242 (2005) 95-9.

Organism

Chlorobium tepidum

Other DBs

ExplorEnz - The Enzyme Database:

1.1.1.153

IUBMB Enzyme Nomenclature:

1.1.1.153

ExPASy - ENZYME nomenclature database:

1.1.1.153

BRENDA, the Enzyme Database:

1.1.1.153

CAS:

9059-48-7

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