Role of Pro-297 in the catalytic mechanism of sheep liver serine hydroxymethyltransferase

Biochemical Journal

Volumn 350, Issue 3, 2000, Pages 849-853

  Talwar, R ^a   Leelavathy, V ^a   Krishna Rao, J V ^a   Appaji Rao, N ^a   Savithri, H S ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

Proton abstraction; Pyridoxal 5' phosphate; Reaction specificity; Site directed mutagenesis

Indexed keywords

ASPARTATE AMINOTRANSFERASE; ASPARTIC ACID; GLYCINE HYDROXYMETHYLTRANSFERASE; LIVER ENZYME; OLIGOMER; PROLINE; PYRIDOXAL 5 PHOSPHATE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; LIVER CYTOSOL; NONHUMAN; PRIORITY JOURNAL; SHEEP; SITE DIRECTED MUTAGENESIS; TRANSAMINATION;

ANIMAL; BASE SEQUENCE; BIOPOLYMERS; CATALYSIS; CIRCULAR DICHROISM; DNA PRIMERS; GLYCINE HYDROXYMETHYLTRANSFERASE; KINETICS; LIVER; PROLINE; SHEEP; SPECTROPHOTOMETRY, ULTRAVIOLET; SUPPORT, NON-U.S. GOV'T;

EID: 0034664977     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3500849     Document Type: Article

References (31)

1. Evolutionary relationships among PLP-dependent enzymes regio-specific α,β and γ families
2. The interconversion of serine and glycine. Participation of pyridoxal-phosphate
3. The crystal structure of human cytosolic serine hydroxymethyltransferase; a target for cancer chemotherapy
4. Crystal structure of rabbit cytosolic serine hydroxymethyltransferase at 2.8 A resolution: Mechanistic implications
5. Molecular organization, catalytic mechanism and function of serine hydroxymethyltransferase - A potential target for cancer chemotherapy
6. Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase
7. The role of lysine-256 in the structure and function of sheep liver recombinant serine hydroxymethyltransferase
8. Function of the active site lysine in E. coli serine hydroxymethyltransferase
9. The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxyrnethyltransferase
10. Role of Arg-401 of cytosolic serine hydroxymethyltransferase in subunit assembly and interaction with the substrate carboxy group
11. Serine hydroxymethyltransferase
12. X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase
13. Tetrahydrofolic acid-5,6,7,8-tetrahydropteroyl-glutamic acid
14. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
15. An efficient vector-primer cDNA cloning system
16. Efficient amplification using 'megaprimer' by asymmetric polymerase chain reaction
17. 3' non-templated 'A' addition by Taq DNA polymerase: An advantage in the construction of single and double mutants
18. DNA sequencing with chain terminating inhibitors
19. Protein measurement with the Folin phenol reagent
20. Purification and physicochemical and regulatory properties of serine hydroxymethyltransferase from sheep liver
21. The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase
22. Serine hydroxymethyttransferase - Transamination of o-alanine
23. Serine hydroxymethyltransferase - Properties of enzyme substrate complexes of D-alanine and glycine
24. Purification and characterization of pyridoxal-5'phosphate dependent serine hydroxymethyltransferase from lamb liver and its action upon β-phenylserine
25. Changing the reaction specificity of a pyddoxal-5'-phosphate-dependent enzyme
26. Interactions of methoxyamine and pyridoxal-5'-phosphate-Schiff's base at the active site of sheep liver sedne hydroxymethyltransferase
27. A novel intermediate in the interaction of thiosemicarbazide with sheep liver serine hydroxymethyltransferase
28. cDNA cloning, overexpression in E. coli purification and characterization of sheep liver cytosolic serine hydroxymethyltransferase
29. His 230 of serine hydroxymethyltransferase facilitates the proton abstraction step in catalysis
30. Asp-89: A critical residue in maintaining the oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase