Beta-hexosaminidase

Details

Name
Beta-hexosaminidase
Synonyms
  • 3.2.1.52
  • Beta-N-acetylhexosaminidase
  • N-acetyl-beta-glucosaminidase
Gene Name
nagZ
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Amino acid sequence
>lcl|BSEQ0020716|Beta-hexosaminidase
MGPLWLDVAGYELSAEDREILQHPTVGGVILFGRNYHDNQQLLALNKAIRQAAKRPILIG
VDQEGGRVQRFREGFSRIPPAQYYARAENGVELAEQGGWLMAAELIAHDVDLSFAPVLDM
GFACKAIGNRAFGEDVQTVLKHSSAFLRGMKAVGMATTGKHFPGHGAVIADSHLETPYDE
RETIAQDMAIFRAQIEAGVLDAMMPAHVVYPHYDAQPASGSSYWLKQVLREELGFKGIVF
SDDLSMEGAAVMGGPVERSHQALVAGCDMILICNKREAAVEVLDNLPIMEVPQAEALLKK
QQFSYSELKRLERWQQASANMQRLIEQFSE
Number of residues
330
Molecular Weight
36465.365
Theoretical pI
5.24
GO Classification
Functions
beta-N-acetylhexosaminidase activity
Processes
carbohydrate metabolic process / cell cycle / cell division / cell wall organization / peptidoglycan biosynthetic process / peptidoglycan turnover / peptidoglycan-based cell wall biogenesis / regulation of cell shape / response to antibiotic
Components
cytoplasm
General Function
Beta-n-acetylhexosaminidase activity
Specific Function
Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. Plays a role in beta-lactam antibiotic resistance via its role in generating anhydro-N-acetylmuramic acid-linked peptides; these peptides function as signaling molecules that induce high-level expression of the beta-lactamase AmpC.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0020717|Beta-hexosaminidase (nagZ)
ATGGGACCGCTTTGGTTGGATGTGGCCGGTTACGAACTGAGTGCCGAAGATCGCGAAATT
CTGCAGCACCCTACAGTGGGTGGTGTGATTCTGTTTGGTCGCAACTATCACGATAACCAG
CAATTGCTGGCACTCAATAAAGCGATCCGTCAAGCGGCGAAAAGACCGATTTTGATTGGT
GTCGATCAAGAAGGTGGCCGCGTGCAGCGTTTCCGTGAAGGCTTTTCTCGCATTCCCCCT
GCGCAGTATTACGCGCGTGCTGAGAATGGCGTTGAGCTTGCTGAGCAGGGCGGTTGGTTG
ATGGCGGCAGAGCTGATTGCACACGATGTTGATTTAAGTTTTGCGCCTGTGCTCGATATG
GGCTTTGCGTGTAAAGCGATTGGCAACCGTGCTTTTGGTGAAGATGTTCAAACTGTACTT
AAGCACAGCAGTGCTTTTCTGCGCGGCATGAAAGCCGTCGGCATGGCGACCACAGGCAAA
CATTTCCCCGGCCATGGCGCGGTGATTGCCGATTCGCATTTAGAGACCCCTTACGATGAG
CGGGAGACGATTGCGCAAGATATGGCGATTTTCCGTGCGCAAATTGAGGCTGGAGTGCTA
GATGCCATGATGCCAGCGCATGTGGTGTATCCGCATTACGATGCTCAACCTGCGAGCGGT
TCGAGCTACTGGCTAAAACAAGTGTTACGTGAAGAACTCGGCTTTAAAGGCATCGTATTT
TCGGATGATTTGAGCATGGAAGGCGCAGCCGTAATGGGGGGGCCAGTTGAGCGCTCCCAT
CAAGCTTTGGTCGCCGGTTGTGACATGATTTTGATCTGTAACAAGCGTGAGGCGGCGGTC
GAAGTGCTGGATAACCTTCCGATCATGGAAGTACCACAAGCTGAAGCACTGCTGAAAAAG
CAGCAATTTAGCTACAGTGAGCTGAAGCGTTTAGAGCGTTGGCAGCAAGCGTCAGCCAAT
ATGCAGCGCTTAATCGAGCAGTTCTCCGAATAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ9KU37
UniProtKB Entry NameNAGZ_VIBCH
GenBank Protein ID9654392
GenBank Gene IDAE003852
General References
  1. Heidelberg JF, Eisen JA, Nelson WC, Clayton RA, Gwinn ML, Dodson RJ, Haft DH, Hickey EK, Peterson JD, Umayam L, Gill SR, Nelson KE, Read TD, Tettelin H, Richardson D, Ermolaeva MD, Vamathevan J, Bass S, Qin H, Dragoi I, Sellers P, McDonald L, Utterback T, Fleishmann RD, Nierman WC, White O, Salzberg SL, Smith HO, Colwell RR, Mekalanos JJ, Venter JC, Fraser CM: DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae. Nature. 2000 Aug 3;406(6795):477-83. [Article]
  2. Stubbs KA, Bacik JP, Perley-Robertson GE, Whitworth GE, Gloster TM, Vocadlo DJ, Mark BL: The development of selective inhibitors of NagZ: increased susceptibility of Gram-negative bacteria to beta-lactams. Chembiochem. 2013 Oct 11;14(15):1973-81. doi: 10.1002/cbic.201300395. Epub 2013 Sep 5. [Article]
  3. Stubbs KA, Balcewich M, Mark BL, Vocadlo DJ: Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance. J Biol Chem. 2007 Jul 20;282(29):21382-91. Epub 2007 Apr 16. [Article]
  4. Balcewich MD, Stubbs KA, He Y, James TW, Davies GJ, Vocadlo DJ, Mark BL: Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ. Protein Sci. 2009 Jul;18(7):1541-51. doi: 10.1002/pro.137. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB07432[[(3R,4R,5S,6R)-3-(butanoylamino)-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-ylidene]amino] N-phenylcarbamateexperimentalunknownDetails
DB08704[[(3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-(pentanoylamino)oxan-2-ylidene]amino] N-phenylcarbamateexperimentalunknownDetails