Literature summary for 1.3.1.98 extracted from

Babajan, B.; Anuradha, C.; Chaitanya, M.; Gowsia, D.; Kumar, C.
In silico structural characterization of Mycobacterium tuberculosis H37Rv UDP-N-acetylmuramate dehydrogenase (2009), Int. J. Integr. Biol., 6, 12-16.

No PubMed abstract available

Search for more literature for 1.3.1.98

Application

Application	Comment	Organism
medicine	computional design of 3-D structures of MurB enzymes and docking studies will provide highly useful information towards rational design of new tuberculosis drugs through experimental research design for further formulations as per pharmaceutical norms	Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment)	Organism
sequence alignment with Escherichia coli structures, PDB entries 2Q85 and 2MBR, and modeling of structure as well as docking with N-acetylpyruvyl glucosamine	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	-	-	-
Mycobacterium tuberculosis	B5AFK3	-	-
Mycobacterium tuberculosis H37Rv	B5AFK3	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-N-acetylenolpyruvylglucosamine + NADPH	complex of MurB and substrate forms strong hydrogen bond with Arg176, Ser257 and Glu361. The secondary structure of MurB consists of 13 helices, 6 beta sheets, 6 beta hairpins, 5 beta bluges, 19 stands, 52 beta turns and 4 inverse gamma turns	Mycobacterium tuberculosis	UDP-N-acetylmuramic acid + NADP+	-	?

Synonyms

Synonyms	Comment	Organism
MurB	-	Mycobacterium tuberculosis

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Mycobacterium tuberculosis

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)