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Literature summary for 2.1.2.1 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
Search for more literature for 2.1.2.1

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q58992
-
-
Methanocaldococcus jannaschii DSM 2661 Q58992
-
-

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Stability [°C]

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

General Information

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