2020
DOI: 10.1074/jbc.ra120.013198
|View full text |Cite
|
Sign up to set email alerts
|

Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase

Abstract: The quinoprotein glycine oxidase from the marine bacterium Pseudoalteromonas luteoviolacea (PlGoxA) uses a protein-derived cysteine tryptophylquinone (CTQ) cofactor to catalyze conversion of glycine to glyoxylate and ammonia. This homotetrameric enzyme exhibits strong cooperativity toward glycine binding. It is a good model for studying enzyme kinetics and cooperativity, specifically for being able to separate those aspects of protein function through directed mutagenesis. Variant proteins were generated with … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

0
2
0

Year Published

2021
2021
2024
2024

Publication Types

Select...
3

Relationship

0
3

Authors

Journals

citations
Cited by 3 publications
(2 citation statements)
references
References 28 publications
0
2
0
Order By: Relevance
“…This homotetrameric enzyme exhibits strong cooperativity toward glycine binding. When the F316A or Y766F mutation at the inter-subunit active-site weakens the glycine binding cooperativity, both the enzyme catalysis potency and the glycine binding potency are also decreased [ 1 ].…”
Section: Introductionmentioning
confidence: 99%
“…This homotetrameric enzyme exhibits strong cooperativity toward glycine binding. When the F316A or Y766F mutation at the inter-subunit active-site weakens the glycine binding cooperativity, both the enzyme catalysis potency and the glycine binding potency are also decreased [ 1 ].…”
Section: Introductionmentioning
confidence: 99%
“…The scaffold also may induce specific ligand geometries and configurations of the reactants not otherwise observed. , In essence, it creates an environment around the active site that can control the atomic distribution of charge and functionality. Variances in redox potentials, the orientation and delivery of reactants, and the energetics of the transition state are all influenced by the local environment surrounding the active site and are typical examples of outer-sphere impacts. ,, …”
Section: Discussionmentioning
confidence: 99%