Literature summary for 2.3.1.157 extracted from

Sulzenbacher, G.; Gal, L.; Peneff, C.; Fassy, F.; Bourne, Y.
Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture (2001), J. Biol. Chem., 276, 11844-11851.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapour-diffusion method. Crystal structures of the enzyme in unbound form, in complex with acetyl-coenzyme A and in complex with both AcCoA and the end product UDP-GlcNAc, determined and refined to 2.3, 2.5, and 1.75 A, respectively. GlmU molecule is organized in two separate domains connected via a long alpha-helical linker and associates as a trimer, with the 50-A-long left-handed beta-helix (LbH) C-terminal domains packed against each other in a parallel fashion and the C-terminal region extended far away from the LbH core and exchanged with the beta-helix from a neighboring subunit in the trimer. AcCoA binding induces the formation of a long and narrow tunnel, enclosed between two adjacent LbH domains and the interchanged C-terminal region of the third subunit, giving rise to an original active site architecture at the junction of three subunits	Streptococcus pneumoniae

Crystallization (Comment)

Organism

hanging-drop vapour-diffusion method. Crystal structures of the enzyme in unbound form, in complex with acetyl-coenzyme A and in complex with both AcCoA and the end product UDP-GlcNAc, determined and refined to 2.3, 2.5, and 1.75 A, respectively. GlmU molecule is organized in two separate domains connected via a long alpha-helical linker and associates as a trimer, with the 50-A-long left-handed beta-helix (LbH) C-terminal domains packed against each other in a parallel fashion and the C-terminal region extended far away from the LbH core and exchanged with the beta-helix from a neighboring subunit in the trimer. AcCoA binding induces the formation of a long and narrow tunnel, enclosed between two adjacent LbH domains and the interchanged C-terminal region of the third subunit, giving rise to an original active site architecture at the junction of three subunits

Streptococcus pneumoniae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-glucosamine 1-phosphate + acetyl-CoA	Streptococcus pneumoniae	the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in bacterial cell wall biosynthesis	N-acetyl-D-glucosamine 1-phosphate + CoA	-	?

Organism

Organism	UniProt	Comment	Textmining
Streptococcus pneumoniae	Q97R46	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glucosamine 1-phosphate + acetyl-CoA	the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in bacterial cell wall biosynthesis	Streptococcus pneumoniae	N-acetyl-D-glucosamine 1-phosphate + CoA	-	?

Synonyms

Synonyms	Comment	Organism
GlmU	bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase	Streptococcus pneumoniae
N-acetylglucosamine-1-phosphate uridyltransferase	bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase	Streptococcus pneumoniae