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Literature summary extracted from

  • Al-Rabiee, R.; Zhang, Y.; Grant, G.A.
    The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase (1996), J. Biol. Chem., 271, 23235-23238.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.95
-
 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.95 H344A 50% inhibition at 0.8 mM L-serine Escherichia coli
1.1.1.95 H344A/N364A no inhibition by L-serine Escherichia coli
1.1.1.95 N346A 50% inhibition at 6 mM L-serine Escherichia coli
1.1.1.95 N346A/H344A no inhibition by L-serine Escherichia coli
1.1.1.95 N346A/N364A no inhibition by L-serine Escherichia coli
1.1.1.95 N364A 50% inhibition at 48 mM L-serine Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.95 (R)-2-amino-1-propanol slightly Escherichia coli
1.1.1.95 amino acids
-
 Escherichia coli
1.1.1.95 beta-Alanine slightly Escherichia coli
1.1.1.95 glycine mutants show less to no inhibition Escherichia coli
1.1.1.95 L-alanine native enzyme and mutant H344A Escherichia coli
1.1.1.95 L-serine 50% inhibition at 0.008 mM L-serine; allosteric inhibition, regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.95 0.038
-
 alpha-ketoglutarate apparent, double mutant H344A/N364A Escherichia coli
1.1.1.95 0.042
-
 alpha-ketoglutarate apparent Escherichia coli
1.1.1.95 0.044
-
 alpha-ketoglutarate apparent, mutant N346A Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.95 3-phosphoglycerate + NAD+ Escherichia coli allosteric inhibition by L-serine, L-serine regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364, 1 serine binds per subunit 3-phosphohydroxypyruvate + NADH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.95 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.95
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.95 3-phosphoglycerate + NAD+
-
 Escherichia coli 3-phosphohydroxypyruvate + NADH
-
 r
1.1.1.95 3-phosphoglycerate + NAD+ allosteric inhibition by L-serine, L-serine regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364, 1 serine binds per subunit Escherichia coli 3-phosphohydroxypyruvate + NADH
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.95 0.128
-
 alpha-ketoglutarate
-
 Escherichia coli
1.1.1.95 0.137
-
 alpha-ketoglutarate double mutant H344A/N364A Escherichia coli
1.1.1.95 0.32
-
 alpha-ketoglutarate mutant N346A Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.95 NAD+
-
 Escherichia coli
1.1.1.95 NADH
-
 Escherichia coli