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PW320824

Pw320824 View Pathway
metabolic

Lipoate Biosynthesis and Incorporation I

Providencia rettgeri DSM 1131
Lipoate is an essential cofactor for key enzymes of oxidative metabolism. Mechanism of lipoate biosynthesis is similar to biotin biosynthesis. Octanoyltransferase facilitates the tranfer of octanoate moiety from octanoate-ACP to particular lysyl residues in lipoate-dependent enzymes. This process regenerates the acyl-carrier in the process, and create an octanylated domains in lipoate-dependent enzymes. Lipoyl synthase combines with S-adenosyl-L-methionine to generate an active lipoylated domain by converting the octanoyl side chain to an active lipoyl. Lipoyl synthase also split S-Adenosyl methionine (AdoMet) into 5'-deoxyadenosyl radical (later becomes 5'-deoxyadenosine by abstracting a hydrogen from a C-H bond) and L-methionine. L-methionine will undergo S-Adenosyl-L-Methionine Biosynthesis.
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: October 08, 2024 at 17:24

Last Updated: October 08, 2024 at 17:24

PW320829

Pw320829 View Pathway
metabolic

Lipoate Biosynthesis and Incorporation I

Providencia stuartii ATCC 25827
Lipoate is an essential cofactor for key enzymes of oxidative metabolism. Mechanism of lipoate biosynthesis is similar to biotin biosynthesis. Octanoyltransferase facilitates the tranfer of octanoate moiety from octanoate-ACP to particular lysyl residues in lipoate-dependent enzymes. This process regenerates the acyl-carrier in the process, and create an octanylated domains in lipoate-dependent enzymes. Lipoyl synthase combines with S-adenosyl-L-methionine to generate an active lipoylated domain by converting the octanoyl side chain to an active lipoyl. Lipoyl synthase also split S-Adenosyl methionine (AdoMet) into 5'-deoxyadenosyl radical (later becomes 5'-deoxyadenosine by abstracting a hydrogen from a C-H bond) and L-methionine. L-methionine will undergo S-Adenosyl-L-Methionine Biosynthesis.
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: October 08, 2024 at 17:27

Last Updated: October 08, 2024 at 17:27

PW320583

Pw320583 View Pathway
metabolic

Lipoate Biosynthesis and Incorporation I

Prevotella pallens ATCC 700821
Lipoate is an essential cofactor for key enzymes of oxidative metabolism. Mechanism of lipoate biosynthesis is similar to biotin biosynthesis. Octanoyltransferase facilitates the tranfer of octanoate moiety from octanoate-ACP to particular lysyl residues in lipoate-dependent enzymes. This process regenerates the acyl-carrier in the process, and create an octanylated domains in lipoate-dependent enzymes. Lipoyl synthase combines with S-adenosyl-L-methionine to generate an active lipoylated domain by converting the octanoyl side chain to an active lipoyl. Lipoyl synthase also split S-Adenosyl methionine (AdoMet) into 5'-deoxyadenosyl radical (later becomes 5'-deoxyadenosine by abstracting a hydrogen from a C-H bond) and L-methionine. L-methionine will undergo S-Adenosyl-L-Methionine Biosynthesis.
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: October 08, 2024 at 15:17

Last Updated: October 08, 2024 at 15:17

PW319719

Pw319719 View Pathway
metabolic

Lipoate Biosynthesis and Incorporation I

Bacteroides fluxus YIT 12057
Lipoate is an essential cofactor for key enzymes of oxidative metabolism. Mechanism of lipoate biosynthesis is similar to biotin biosynthesis. Octanoyltransferase facilitates the tranfer of octanoate moiety from octanoate-ACP to particular lysyl residues in lipoate-dependent enzymes. This process regenerates the acyl-carrier in the process, and create an octanylated domains in lipoate-dependent enzymes. Lipoyl synthase combines with S-adenosyl-L-methionine to generate an active lipoylated domain by converting the octanoyl side chain to an active lipoyl. Lipoyl synthase also split S-Adenosyl methionine (AdoMet) into 5'-deoxyadenosyl radical (later becomes 5'-deoxyadenosine by abstracting a hydrogen from a C-H bond) and L-methionine. L-methionine will undergo S-Adenosyl-L-Methionine Biosynthesis.
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: October 08, 2024 at 02:29

Last Updated: October 08, 2024 at 02:29

PW319707

Pw319707 View Pathway
metabolic

Lipoate Biosynthesis and Incorporation I

Bacteroides cellulosilyticus DSM 14838
Lipoate is an essential cofactor for key enzymes of oxidative metabolism. Mechanism of lipoate biosynthesis is similar to biotin biosynthesis. Octanoyltransferase facilitates the tranfer of octanoate moiety from octanoate-ACP to particular lysyl residues in lipoate-dependent enzymes. This process regenerates the acyl-carrier in the process, and create an octanylated domains in lipoate-dependent enzymes. Lipoyl synthase combines with S-adenosyl-L-methionine to generate an active lipoylated domain by converting the octanoyl side chain to an active lipoyl. Lipoyl synthase also split S-Adenosyl methionine (AdoMet) into 5'-deoxyadenosyl radical (later becomes 5'-deoxyadenosine by abstracting a hydrogen from a C-H bond) and L-methionine. L-methionine will undergo S-Adenosyl-L-Methionine Biosynthesis.
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: October 08, 2024 at 02:22

Last Updated: October 08, 2024 at 02:22

PW002107

Pw002107 View Pathway
metabolic

Lipoate Biosynthesis and Incorporation I

Escherichia coli
Lipoate is an essential cofactor for key enzymes of oxidative metabolism. Mechanism of lipoate biosynthesis is similar to biotin biosynthesis. Octanoyltransferase facilitates the tranfer of octanoate moiety from octanoate-ACP to particular lysyl residues in lipoate-dependent enzymes. This process regenerates the acyl-carrier in the process, and create an octanylated domains in lipoate-dependent enzymes. Lipoyl synthase combines with S-adenosyl-L-methionine to generate an active lipoylated domain by converting the octanoyl side chain to an active lipoyl. Lipoyl synthase also split S-Adenosyl methionine (AdoMet) into 5'-deoxyadenosyl radical (later becomes 5'-deoxyadenosine by abstracting a hydrogen from a C-H bond) and L-methionine. L-methionine will undergo S-Adenosyl-L-Methionine Biosynthesis.
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Ana Marcu

Created On: October 14, 2015 at 11:32

Last Updated: October 14, 2015 at 11:32

PW123571

Pw123571 View Pathway
metabolic

Lipoate Biosynthesis and Incorporation I

Pseudomonas aeruginosa
Lipoate is an essential cofactor for key enzymes of oxidative metabolism. Mechanism of lipoate biosynthesis is similar to biotin biosynthesis. Octanoyltransferase facilitates the tranfer of octanoate moiety from octanoate-ACP to particular lysyl residues in lipoate-dependent enzymes. This process regenerates the acyl-carrier in the process, and create an octanylated domains in lipoate-dependent enzymes. Lipoyl synthase combines with S-adenosyl-L-methionine to generate an active lipoylated domain by converting the octanoyl side chain to an active lipoyl. Lipoyl synthase also split S-Adenosyl methionine (AdoMet) into 5'-deoxyadenosyl radical (later becomes 5'-deoxyadenosine by abstracting a hydrogen from a C-H bond) and L-methionine. L-methionine will undergo S-Adenosyl-L-Methionine Biosynthesis.
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Ana Marcu

Created On: August 12, 2019 at 22:32

Last Updated: August 12, 2019 at 22:32

PW319319

Pw319319 View Pathway
metabolic

Lipoate Biosynthesis and Incorporation I

Alistipes shahii WAL 8301
Lipoate is an essential cofactor for key enzymes of oxidative metabolism. Mechanism of lipoate biosynthesis is similar to biotin biosynthesis. Octanoyltransferase facilitates the tranfer of octanoate moiety from octanoate-ACP to particular lysyl residues in lipoate-dependent enzymes. This process regenerates the acyl-carrier in the process, and create an octanylated domains in lipoate-dependent enzymes. Lipoyl synthase combines with S-adenosyl-L-methionine to generate an active lipoylated domain by converting the octanoyl side chain to an active lipoyl. Lipoyl synthase also split S-Adenosyl methionine (AdoMet) into 5'-deoxyadenosyl radical (later becomes 5'-deoxyadenosine by abstracting a hydrogen from a C-H bond) and L-methionine. L-methionine will undergo S-Adenosyl-L-Methionine Biosynthesis.
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: October 07, 2024 at 22:50

Last Updated: October 07, 2024 at 22:50

PW357124

Pw357124 View Pathway
metabolic

Lipoate Biosynthesis and Incorporation I

Escherichia coli O157:H7 str. EC4115
Lipoate is an essential cofactor for key enzymes of oxidative metabolism. Mechanism of lipoate biosynthesis is similar to biotin biosynthesis. Octanoyltransferase facilitates the tranfer of octanoate moiety from octanoate-ACP to particular lysyl residues in lipoate-dependent enzymes. This process regenerates the acyl-carrier in the process, and create an octanylated domains in lipoate-dependent enzymes. Lipoyl synthase combines with S-adenosyl-L-methionine to generate an active lipoylated domain by converting the octanoyl side chain to an active lipoyl. Lipoyl synthase also split S-Adenosyl methionine (AdoMet) into 5'-deoxyadenosyl radical (later becomes 5'-deoxyadenosine by abstracting a hydrogen from a C-H bond) and L-methionine. L-methionine will undergo S-Adenosyl-L-Methionine Biosynthesis.
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: November 12, 2024 at 12:25

Last Updated: November 12, 2024 at 12:25

PW320695

Pw320695 View Pathway
metabolic

Lipoate Biosynthesis and Incorporation I

Parasutterella excrementihominis YIT 11859
Lipoate is an essential cofactor for key enzymes of oxidative metabolism. Mechanism of lipoate biosynthesis is similar to biotin biosynthesis. Octanoyltransferase facilitates the tranfer of octanoate moiety from octanoate-ACP to particular lysyl residues in lipoate-dependent enzymes. This process regenerates the acyl-carrier in the process, and create an octanylated domains in lipoate-dependent enzymes. Lipoyl synthase combines with S-adenosyl-L-methionine to generate an active lipoylated domain by converting the octanoyl side chain to an active lipoyl. Lipoyl synthase also split S-Adenosyl methionine (AdoMet) into 5'-deoxyadenosyl radical (later becomes 5'-deoxyadenosine by abstracting a hydrogen from a C-H bond) and L-methionine. L-methionine will undergo S-Adenosyl-L-Methionine Biosynthesis.
BioPAX SVG SBGN SBML PWML All files (.zip)

Creator: Julia Wakoli

Created On: October 08, 2024 at 16:16

Last Updated: October 08, 2024 at 16:16