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Information on EC 6.3.4.11 - biotin-[methylcrotonoyl-CoA-carboxylase] ligase

for references in articles please use BRENDA:EC6.3.4.11

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EC Tree

6 Ligases

6.3 Forming carbon-nitrogen bonds

6.3.4 Other carbon-nitrogen ligases

6.3.4.11 biotin-[methylcrotonoyl-CoA-carboxylase] ligase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

Reaction Schemes

apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]

AMP

diphosphate

[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]

Synonyms

Beta-methylcrotonyl coenzyme A holocarboxylase synthetase, Biotin-beta-methylcrotonyl coenzyme A carboxylase synthetase, Biotin-[methylcrotonyl-CoA-carboxylase] synthetase, Synthetase, biotin-beta-methylcrotonyl coenzyme A carboxylase, show all synonyms

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SYNONYM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Beta-methylcrotonyl coenzyme A holocarboxylase synthetase

Biotin-beta-methylcrotonyl coenzyme A carboxylase synthetase

Biotin-[methylcrotonyl-CoA-carboxylase] synthetase

Synthetase, biotin-beta-methylcrotonyl coenzyme A carboxylase

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

ATP + biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]

3 entries

ATP + biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]

the first reaction step is the reversible formation of biotinyl adenylate, the biotin residue is transferred to the apoenzyme in a second step

Achromobacter sp.

1398

ATP + biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]

the first reaction step is the reversible formation of biotinyl adenylate, the biotin residue is transferred to the apoenzyme in a second step

Achromobacter sp. IVS-W

ATP + biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]

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REACTION TYPE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

amination

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PATHWAY SOURCE

PATHWAYS

KEGG

Biotin metabolism

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SYSTEMATIC NAME

IUBMB Comments

biotin:apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] ligase (AMP-forming)

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CAS REGISTRY NUMBER

COMMENTARY

37318-68-6

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SUBSTRATE

PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

Reversibility
r=reversible
ir=irreversible
?=not specified

ATP + biotin + apo-[3-methylcrotonyl-CoA:carbondioxide ligase (ADP-forming)]

AMP + diphosphate + [3-methylcrotonyl-CoA:carbondioxide ligase (ADP-forming)]

3 entries

ATP + biotin + apo-[3-methylcrotonyl-CoA:carbondioxide ligase (ADP-forming)]

AMP + diphosphate + [3-methylcrotonyl-CoA:carbondioxide ligase (ADP-forming)]

Achromobacter sp.

biotin is transferred specifically to the epsilon-amino groups of lysine residues located in apocenters

1398

ATP + biotin + apo-[3-methylcrotonyl-CoA:carbondioxide ligase (ADP-forming)]

AMP + diphosphate + [3-methylcrotonyl-CoA:carbondioxide ligase (ADP-forming)]

Achromobacter sp. IVS-W

biotin is transferred specifically to the epsilon-amino groups of lysine residues located in apocenters

1398

ATP + biotin + apo-[3-methylcrotonyl-CoA:carbondioxide ligase (ADP-forming)]

AMP + diphosphate + [3-methylcrotonyl-CoA:carbondioxide ligase (ADP-forming)]

Propionibacterium freudenreichii subsp. shermanii

1398

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Mg2+

Achromobacter sp.

required

1398

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

Achromobacter sp.

1398

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Achromobacter sp.

1398

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

7.4 - 8.5

Achromobacter sp.

85% of maximal activity at pH 7.4 and 8.5

1398

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Achromobacter sp.

IVS-W

1398

brenda

Achromobacter sp. IVS-W

IVS-W

1398

brenda

Propionibacterium freudenreichii subsp. shermanii

1398

brenda

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

P50747 pBLAST

BPL1_HUMAN

Homo sapiens

726

80760

Swiss-Prot