Role of the conserved Ser-Tyr-Lys triad of the SDR family in sepiapterin reductase

Chemico-Biological Interactions

Volumn 130-132, Issue , 2001, Pages 825-832

  Fujimoto, Kengo ^a   Hara, Masayuki ^a   Yamada, Hirotaka ^a   Sakurai, Masato ^a   Inaba, Akemi ^a   Tomomura, Akito ^a   Katoh, Setsuko ^a  

^a MEIKAI UNIVERSITY SCHOOL OF DENTISTRY   (Japan)

Author keywords

Conserved Ser Tyr Lys triad; Point mutants; Sepiapterin reductase

Indexed keywords

SEPIAPTERIN; SEPIAPTERIN REDUCTASE; TETRAHYDROBIOPTERIN;

AMINO ACID SEQUENCE; CATALYSIS; CONFERENCE PAPER; ENZYME ACTIVITY; NONHUMAN; POINT MUTATION; PROTON TRANSPORT; RAT; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ALCOHOL OXIDOREDUCTASES; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CONSERVED SEQUENCE; DNA PRIMERS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RATS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 0035969849     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(00)00238-6     Document Type: Conference Paper

References (15)

1. Sepiapterin reductase exhibits a NADPH-dependent dicarbonyl reductase activity
2. Carbonyl reductase activity of sepiapterin reductase from rat erythrocytes
3. The complete amino acid sequence of the mature form of rat sepiapterin reductase
4. Cloning and sequencing of cDNA encoding human sepiapterin reductase: An enzyme involved in tetrahydrobiopterin biosynthesis
5. Mouse sepiapterin reductase: An enzyme involved in the final step of tetrahydrobiopterin biosynthesis. Primary structure deduced from the cDNA sequence
6. Short-chain dehydrogenases/reductases (SDR)
7. Functionally important residues tyrosine-171 and serine-158 in sepiapterin reductase
8. Comparative anatomy of the aldo-keto reductase superfamily
9. 2+-dependent phosphorylation and proteolysis of tetrahydrobiopterin generating enzymes
10. Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: The structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family
11. Crystal structure of the binary and ternary complexes of 7α-hydroxysterold dehydrogenase from Escherichia coli
12. The 1.25 Å crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters
13. Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4-isomerase from Escherichia coli
14. Dyspropterin, an intermediate formed from dihydroneopterin triphosphate in the biosynthetic pathway of tetrahydrobiopterin
15. Coenzyme stimulation of isomerase activity of sepiapterin reductase in the biosynthesis of tetrahydrobiopterin