Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: evidence for cooperativity in biotin carboxylase (Q28244931)

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scientific article (publication date: 16 April 2004)

Language	Label	Description	Also known as
English	Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: evidence for cooperativity in biotin carboxylase	scientific article (publication date: 16 April 2004)

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scholarly article

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Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: evidence for cooperativity in biotin carboxylase (English)

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propionic acidemia

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based on heuristic

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author name string

Valerie Sloane

1

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Grover L Waldrop

2

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language of work or name

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publication date

16 April 2004

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Journal of Biological Chemistry

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279

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16

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15772-8

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1 reference

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The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency

1 reference

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Coding sequence mutations in the alpha subunit of propionyl-CoA carboxylase in patients with propionic acidemia

1 reference

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Functional characterization of PCCA mutations causing propionic acidemia.

1 reference

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Functional analysis of MCCA and MCCB mutations causing methylcrotonylglycinuria.

1 reference

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1 reference

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1 reference

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Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase

1 reference

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Movement of the biotin carboxylase B-domain as a result of ATP binding

1 reference

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ATPase activity of biotin carboxylase provides evidence for initial activation of HCO3- by ATP in the carboxylation of biotin.

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Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer

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Proteomics and models for enzyme cooperativity.

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Metabolic stroke in isolated 3-methylcrotonyl-CoA carboxylase deficiency.

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ALSCRIPT: a tool to format multiple sequence alignments

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Overview of mutations in thePCCA andPCCB genes causing propionic acidemia

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Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin

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Do cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of biotin?

1 reference

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Inhibition of biotin carboxylase by a reaction intermediate analog: implications for the kinetic mechanism

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Conversion of Non-allosteric Pyruvate Kinase Isozyme into an Allosteric Enzyme by a Single Amino Acid Substitution

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21 January 2018

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10.1074/JBC.M311982200

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