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Literature summary for 3.5.1.44 extracted from

  • Kumeta, H.; Miwa, N.; Ogura, K.; Kai, Y.; Mizukoshi, T.; Shimba, N.; Suzuki, E.; Inagaki, F.
    The NMR structure of protein-glutaminase from Chryseobacterium proteolyticum (2010), J. Biomol. NMR, 46, 251-255.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Corynebacterium glutamicum Chryseobacterium proteolyticum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
19860
-
calculated from amino acid sequence Chryseobacterium proteolyticum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Chryseobacterium proteolyticum protein-glutaminase catalyzes only the deamidation of the side chain amido group of protein-bound glutaminyl residues to release ammonia without catalyzing the transglutamination and hydrolysis of asparaginyl residues or producing other undesirable changes in protein structure ?
-
?

Organism

Organism UniProt Comment Textmining
Chryseobacterium proteolyticum
-
strain 9670
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information protein-glutaminase catalyzes only the deamidation of the side chain amido group of protein-bound glutaminyl residues to release ammonia without catalyzing the transglutamination and hydrolysis of asparaginyl residues or producing other undesirable changes in protein structure Chryseobacterium proteolyticum ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 19860, calculated from amino acid sequence Chryseobacterium proteolyticum

Synonyms

Synonyms Comment Organism
protein-glutaminase
-
Chryseobacterium proteolyticum

pI Value

Organism Comment pI Value Maximum pI Value
Chryseobacterium proteolyticum calculated from amino acid sequence
-
10