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MUTANT ACCESSION NUMBER: 61
PROTEIN NAME: Serine hydroxymethyltransferase, cytosolic (EC 2.1.2.1) (Serine methylase) (Glycine hydroxymethyltransferase) (SHMT).
SWISS PROT ENTRY: GLYC_SHEEP
ORGANISM: OVIS ARIES SHEEP
GENE NAME: SHMT1
VARIANT OR MUTAGEN:Mutagen
PMD ENTRY: A993462

MUTATIONS: 
POINT Asp 89 Asn

EFFECTS: Secondary structure [=] (by far-UV CD spectrum): When purified in the presence of PLP, the D89N SHTM is a mixture of dimers and tetramers with the proportion of tetramers increasing with an increase in PLP concentration used during purification. (The wild-type SHTM is purified as a tetramer.): The apo-form of the D89N SHTM is a dimer unlike the apo-form of the wild- type SHTM which is present predominantly as a tetramer.: The apo mutant dimer can not be reconstituted to the holo-form by the addition of excess of PLP. FUNCTION Specific activity of the D89N dimer in the absence of PLP [-] and in the presence of PLP [-]: Formation of the quinonoid spectral intermediate in the reaction of the D89N dimer with glycine and H4-folate [0]: Specific activity of the D89N tetramer in the absence of PLP [-] and in the presence of PLP [=]: For the D89N tetramer, Km [=], kcat [-] and kcat/Km [-] for serine in the absence of PLP: For the D89N tetramer, Km [=], kcat [=] and kcat/Km [=] for serine in the presence of PLP: Formation of the quinonoid spectral intermediate in the reaction of the D89N tetramer with glycine and H4-folate [-] STABILITY Thermal stability of D89N tetramer in the presence of PLP [-] (as indicated by Tm): Thermal stability of the D89N tetramer is markedly increased by addition of serine, as in the case of the wild-type SHTM.: There is no change in the thermal stability of the D89N dimer in the presence and absence of serine.

REFERENCE:
PUBMED ID: 10493937
TITLE:Asp-89: a critical residue in maintaining the oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase
AUTHOR:Krishna Rao JV, Jagath JR, Sharma B, Appaji Rao N, Savithri HS.
REFERENCE:Biochem J. 1999 Oct 1;343 Pt 1:257-63.

3D STRUCTURE: Null

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