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Links from Protein

Items: 9

1.

Glutaminase/Asparaginase C-terminal domain

This domain is found at the C-terminus of asparaginase enzymes. [1]. 16216574. Structural basis for tRNA-dependent amidotransferase function. Schmitt E, Panvert M, Blanquet S, Mechulam Y;. Structure. 2005;13:1421-1433. (from Pfam)

Date:
2024-10-16
Family Accession:
NF036996.5
Method:
HMM
2.

asparaginase domain-containing protein

This is the N-terminal domain of this enzyme. (from Pfam)

Date:
2024-08-14
Family Accession:
NF012913.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

asparaginase

asparaginase catalyzes the formation of aspartate from asparagine, periplasmic

Date:
2017-03-27
Family Accession:
10013725
Method:
Sparcle
8.

L-asparaginase 2

Catalyzes the formation of aspartate from asparagine

Gene:
ansB
GO Terms:
Molecular Function:
asparaginase activity (GO:0004067)
Biological Process:
asparagine metabolic process (GO:0006528)
Date:
2021-10-13
Family Accession:
NF008304.0
Method:
HMM
9.

type II asparaginase

Two related families of asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity periplasmic enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type II of E. coli. Both the cytoplasmic and the cell wall asparaginases of Saccharomyces cerevisiae belong to this set. Members of this set from Acinetobacter glutaminasificans and Pseudomonas fluorescens are described as having both glutaminase and asparaginase activitities. All members are homotetrameric.

GO Terms:
Molecular Function:
asparaginase activity (GO:0004067)
Biological Process:
asparagine metabolic process (GO:0006528)
Date:
2021-09-08
Family Accession:
TIGR00520.1
Method:
HMM
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