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Literature summary extracted from

  • Angelucci, F.; Morea, V.; Angelaccio, S.; Saccoccia, F.; Contestabile, R.; Ilari, A.
    The crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures (2014), Proteins, 82, 3437-3449.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.2.1 crystal structure of the apoenzyme and pyridoxal 5'-phosphate-bound holoenzyme at 2.83 and 3.0 A resolution, respectively. The crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Methanocaldococcus jannaschii Q58992
-
-
2.1.2.1 Methanocaldococcus jannaschii DSM 2661 Q58992
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 NADH + coenzyme Q10
-
 Methanocaldococcus jannaschii ?
-
 ?
2.1.2.1 NADH + coenzyme Q10
-
 Methanocaldococcus jannaschii DSM 2661 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 MJ1597 locus name Methanocaldococcus jannaschii
2.1.2.1 serine hydroxymethyltransferase
-
 Methanocaldococcus jannaschii
2.1.2.1 SHMT
-
 Methanocaldococcus jannaschii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.2.1 additional information
-
 the crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures Methanocaldococcus jannaschii

General Information

EC Number General Information Comment Organism
2.1.2.1 metabolism the enzyme plays an essential role in one-carbon unit metabolism Methanocaldococcus jannaschii