EC number:2.1.2.1

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.2 Hydroxymethyl-, formyl- and related transferases
ID:2.1.2.1
Description:Glycine hydroxymethyltransferase.
Alternative Name: Threonine aldolase.
Serine hydroxymethyltransferase.
Serine hydroxymethylase.
Serine aldolase.
Prosite: PDOC00090;
PDB:
PDBScop
1LS3 8026574; 8038953; 8026574; 8038953; 8026574; 8038953; 8026574; 8038953;
1RVY 8026574; 8038953; 8026574; 8038953;
1RVU 8026574; 8038953; 8026574; 8038953;
1RV4 8026574; 8038953; 8026574; 8038953;
1CJ0 8026574; 8038953; 8026574; 8038953;
 » show all
Cath: 3.40.640.10; 3.90.1150.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.2.1
BRENDA Enzyme Link: BRENDA 2.1.2.1
KEGG Enzyme Link: KEGG2.1.2.1
BioCyc Enzyme Link: BioCyc 2.1.2.1
ExPASy Enzyme Link: ExPASy2.1.2.1
EC2PDB Enzyme Link: EC2PDB 2.1.2.1
ExplorEnz Enzyme Link: ExplorEnz 2.1.2.1
PRIAM enzyme-specific profiles Link: PRIAM 2.1.2.1
IntEnz Enzyme Link: IntEnz 2.1.2.1
MEDLINE Enzyme Link: MEDLINE 2.1.2.1

EC number:2.1.2.1

MSA:

2.1.2.1;
Phylogenetic Tree:

2.1.2.1;
Uniprot:
M-CSA:
RHEA:15481 (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]-[N;H0;+0:5]1-[*:6]-[*:7]-[N;H0;+0:8](-[*:9])-[CH2;+0:10]-1.[OH2;+0:11]>>[*:1]-[CH;+0:2](-[*:3])-[CH2;+0:10]-[OH;+0:11].[*:4]-[NH;+0:5]-[*:6]-[*:7]-[NH;+0:8]-[*:9]
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References

TitleAuthorsDatePubMed ID
Purification and properties of serine hydroxymethylase from soluble and mitochondrial fractions of rabbit liver.Fujioka M19695808700
Serine transhydroxymethylase. Identification as the threonine and allothreonine aldolases.Schirch L, Gross T1968 Nov 105699057
Inactivation of serine transhydroxymethylase and threonine aldolase activities.Akhtar M, el-Obeid HA1972 Mar 85017703
Threonine aldolase from Candida humicola. II. Purification, crystallization and properties.Kumagai H, Nagate T, Yoshida H, Yamada H1972 Mar 85017702
A spectrophotometric study of the reaction catalysed by serine transhydroxymethylase.Blakley RL1960 Dec16748851